Morgellons & Carbon Monoxide

Morgellons & Carbon Monoxide

by
Clifford E Carnicom
Aug 14 2016
(To Be Continued)

Note: I am not offering any medical advice or diagnosis with the presentation of this information. I am acting solely as an independent researcher providing the results of extended observation and analysis of unusual biological conditions that are evident.  Each individual must work with their own health professional to establish any appropriate course of action and any health related comments in this paper are solely for informational purposes and they are from my own perspective.

Methods have been developed that confirm the existence of carbon monoxide gas production by the microorganism identified as a source of the “Morgellons” condition.  The existence of this gas as a repeatable and identifiable phenomenon from the metabolism of the microorganism poses a host of serious health implications to consider.

The presence of the gas during growth was first established and identified with the methods of gas chromatography.  Carbon dioxide production is in the majority proportion and carbon monoxide accompanies this in a lower proportion, as is shown below.

CDB CO2_CO Production2

Reference gas chromatogram depicting a comparison between carbon dioxide and carbon monoxide isolated from automobile exhaust and that of the microorganism (CDB).  Retention times correspond and support the identification of both carbon dioxide and carbon monoxide production.

As described in previous papers, the tentative nomenclature for the microorganism has been designated as a “cross-domain bacteria“, or CDB.  This terminology remains in place by this researcher as study continues; all evidence does continue to support the hypothesis of a predominant bacterial origin and nature.

The conclusions regarding the gas as a product of metabolism have been further confirmed with the use of infrared spectrometry.  The carbon dioxide spectrum (gas) presents strong absorbance peaks in the 2100 – 2200 cm-1 wavenumber range.  These peaks have been repeatedly identified within the gaseous samples from the CDB microorganism.

CDB Gas Production CO Segment Average Aug 13 2016 - 13

Infrared spectrum of the gaseous metabolic product from the CDB.  Absorbance in the 2100 – 2200 cm-1 wavenumber range has been repeatedly identified, and is shown above.  This absorbance in this specific infrared range further supports the conclusion of carbon monoxide production by the microorganism.

CO2_NIST_Gas

 Reference spectrum of gaseous carbon monoxide.  Absorbance in the 2100-2200 cm-1 wavenumber range exists as a unique identifying characteristic of the gas.  Source of image : NIST

Gas chromatography and infrared spectrometry methods, applied repeatedly to multiple samples of CDB growth, both support the conclusions of carbon dioxide and carbon monoxide production reached in this report.

The concentration of carbon dioxide within the samples is relatively high and easily detected.  The concentration of carbon monoxide is lower, and is at roughly the limits of detection with the instrumentation available.  A first and partial estimate of the carbon monoxide concentration is on the order of 50-100 parts per million (ppm) within the sample volumes examined.  The existence of continuous gas production by the CDB, irrespective of concentrations to be determined in the future, is sufficient to warrant serious health impact investigations.

Additional gaseous production, such as that from hydrocarbons, remains an additional topic of investigation and remains for future discussions.

The primary purpose of this paper is to disclose the result in preparation for future examinations.  A few historical and leading comments will be made with respect to the health issues that warrant mention, but this topic is obviously deserving of its own discussion in future days.

The finding is, of course, of significance.  However, for those familiar with the history of research on this site, the disclosure should not be one of total surprise.  There is now a record over several years of an ongoing chronicle of reported and expected interference with major systems of the body from the Morgellons condition.  This interference and damage to human health most emphatically concerns all aspects of energy production, oxygen transport, iron utilization and respiration.  It has been reported on continuously for a period of many years now.  What differs in the the current situation is that a primary mechanism for a portion of that harm may be under definition.

I will spare the reader of citing the legacy of work on this site that is completely and totally consistent with a finding of carbon monoxide within the metabolism of the organism; I do, however, encourage that investigation to understand the depth of work that leads us to this occasion.

The most immediate need will be a preview to some of the potential health risks from carbon monoxide in the body.  I would suggest that a focal point of investigation be that of chronic low level exposure and the associated symptoms and conditions that might result. Higher concentration impacts, for a myriad of practical reasons, would not seem to be relevant at this time. Carbon monoxide and human health is serious business no matter how you choose to look at it.   It will also be of interest in our future to compare the low level exposure symptoms with those that will, in due time, become known from the investigative survey (MRP) conducted by this Institute.  The investigations will be complicated further by the broad array of disruptors that been brought forth in the course of the research over many years.

It will also be of interest to investigate those groups of bacteria or related microorganisms that share in the property of producing carbon monoxide, carbon dioxide, and/or various hydrocarbons within their metabolism.  The commonality of that trait will also be of interest.

Let us look at the latter question first.

To Be Continued

Morgellons Research: Proteinaceous Complex Identified

Morgellons Research:
Proteinaceous Complex Identified

Clifford E Carnicom
Mar 14 2012
This paper is subject to edits.

Note: I am not offering any medical advice or diagnosis with the presentation of this information. I am acting solely as an independent researcher providing the results of extended observation and analysis of unusual biological conditions that are evident.  Each individual must work with their own health professional to establish any appropriate course of action and any health related comments in this paper are solely for informational purposes and they are from my own perspective.

A proteinaceous complex that derives from oral filament cultures has been identified. This finding, along with the significant presence of iron within the same culture growths, is paramount in the understanding of the physical nature of the filaments characteristic of the condition.

The method of determination of this complex has been protracted and difficult, primarily because of the lack of resources that are available to achieve a more direct knowledge of composition.  The work has been conducted over a period of several months, and the results have been arrived at through a combination of deductive methods, qualitative chemical tests, column chromatography, analytical chemical separation techniques, and visible light spectroscopy.  Methods of thin layer chromatography, distillation and electrophoresis have also been included.   Additional resources, should they become available, can hasten the process of discovery which remains in midstream.  This declaration itself has been on hold for more than two months, until the opportunity of presentation has afforded itself.

To give an example of the importance of protein discoveries, the success in curtailment of harm from the AIDs virus has been accomplished largely from the massive efforts that have been made to understand the protein complexes involved.  Proteins, upon discovery of uniqueness, are themselves patentable and are the basis of much of the pharmaceutical industry.  This exists as a controversial subject in its own right.  With the proper equipment and resources, many of the questions and problems posed by the topic of this paper could be answered directly and promptly.

Proteins are classically designated as the “building blocks” of nature.  It is quite common for approximately one-half of the composition of an organism to be of proteins.  Understanding this aspect of the filament nature of the Morgellons condition is obviously of the highest priority of any biochemical research project; to date, however, this information has been essentially non-existent or scant.  

A recent report by the Centers for Disease Control (CDC) raises the ante of this controversy by themselves declaring a significant percentage of the materials studied to be composed of proteins.  The report subsequently proceeds to ignore any direct presentation of laboratory results and strategically uses terms such as “likely” and “similar” versus a direct presentation of chemical composition to the molecular level, as is required. The report also eventually leads to a pre-directed “conclusion” that transforms the physical presence of these proteins into the metaphysical world and classifies the manifestation of this physical and laboratory presence as a continuing “delusional” condition.  

As another illustration of the inexcusable delay and failings of this report, let it be known that when a critical and unexpected health situation arrived on the scene some time ago, namely the Hantavirus crisis, the CDC had the issue contained, sourced and identified within a couple of weeks of investigation.  Six years later, several hundred thousand dollars more, in question of collusion with the Armed Forces of Pathology, and we remain at the same and exact original point of agenda driven policy.  This shirk from proper investigation and disclosure of factual results is a disservice to the public welfare, benefit, interest and health.

Suffice it to say that the objective of the scientific method is to test and resolve a hypothesis, and that it is not to “generate hypotheses” as a primary goal.  Such thinking is to encourage the arena of speculation and obfuscation versus resolution, which is exactly what has been accomplished with the recent report.  This is not science.  The reader is requested to read the report from a analytical, objective, scientific and critical thinking perspective and not to be duped by the vagaries and critical exclusions that are apparent within the so-called “report.”  The ludicrousness of the CDC report and the abject failure to adhere to the principles of scientific resolution will not be discussed further here.  

This researcher will now proceed, from a base of limited resources, to describe the laboratory results that derive from the efforts of the Carnicom Institute.  The writer fully acknowledges that many difficulties remain and that many questions remain unanswered.  Certainly some very specific information desperately needed can not be had at this point.  The writer allows for the possibility of error and insists that further verification or refutation of the work is required.  It is, nevertheless, the state of knowledge apparent at this time.

The most succinct description of the proteinaceous complex that can be provided at this time is as follows:

An apparent metalloid dipeptide complex, likely composed of an coordinated ferric iron (III) complex.  The amino acid cysteine appears to be dominant in the composition.  There is also evidence emerging for the presence of histidine.  The most likely dipeptide forms are therefore cysteine-cysteine (i.e., cystine form) or a cysteine-histidine iron dipeptide complex.  Additional amino acids will remain a part of the investigation, as well as the variability in the spectrums as a function of pH.

There may be error within this assessment of the nature of the complex, but it is believed at this point to be an accurate statement.  There are intellectual property issues that may at some point become involved with the statement made above.  The Institute is fully aware of the importance of, and economic value of, protein identification and potential discovery.  The Institute at this time, however, does not possess the means or resources to evaluate the complex at the molecular level, which is required.  Equally, the means to pursue patent interests or protection does not exist and pharmaceutical interests may eventually emerge.  The Institute will instead place its focus on the disclosure of information that serves the public benefit and welfare, such that further and needed urgent research can take place.  The Institute is on record as opposing any proprietary developments that may develop from this research without the involvement of the Carnicom Institute.  The public health interest and welfare is to remain as the paramount goal.

Let us discuss the methods by which this conclusion has been made.  In all, more than a half dozen different techniques or methods have been used to arrive at the above statement.  These are:

1. Extended observation and analysis of a column chromatography process of separation of the protein complex from a prepared culture solution.  In particular, the interaction of the culture with copper salts became an important factor in the process of identification.

2. The use of the qualitative biuret test for proteins.

3. Spectral analysis of a control solution of a dipeptide compared to the spectral analysis of the proteinaceous complex under study.

4. The use of ninhydrin applied to a solution of the complex on filter paper and then heated.

5. The reactions of a control set of amino acids, by color, upon heating in a ninhydrin solution.

6. The spectral analysis of the same set of control amino acids mentioned above.

7. The behavior of the proteinaceous complex when subject to N-acetyl cysteine and ninhydrin.

8. A positive test for the existence of iron after reduction by N-acetyl cysteine.

9. A spectral comparison of the amino acid cysteine with the proteinaceous complex under the condition of reduction and in combination with a heated ninhydrin solution.

Let us briefly describe each of these factors to gain a better understanding of how the assessment has been achieved.  A strong reliance on a series of photographs will be made to summarize the complex process that is described above.

chromatography
 A chromatography column in operation.

1. Column Chromatography:

A great deal of time and effort has been devoted to the development of column chromatography methods and techniques as it applies to the decomposition problem.  Column chromatography is a method of separation of a mixture into various constituent components.  A great deal of trial and error is required to develop a successful column.  This has been achieved with a fair degree of reliability at this point in the research.

The specific details of proteinaceous eluate extraction will not be described in detail here.  Many combinations of solvents, salt solutions, and adbsorbents have been used to eventually produce the proteinaceous eluate under study here.  What can be stated is that a particular reaction of the culture solutions with copper salts is indeed of high interest.  It will be found that blue copper protein compounds can be formed with the proper combination of the culture solution, copper salts. solvents, and adsorbents (stationary phase).  The blue copper proteins have particular chemical compositional qualities, a majority of them that involve the amino acids of cysteine and histidine (Type I Blue Copper Proteins).  This phase of the research was the first indication of specific amino acids that may be involved in the composition, and it led to an early interest in the specific amino acids of histidine and cysteine as a part of the composition.

proteinaceous eluate
The proteinaceous eluate extracted from the chromatography column. It requires approximately two weeks of column chromatography to produce this volume.

 

2. The Biuret Test is an important test for the existence of proteins and peptide bonds.  It can be used in both a qualitative and a quantitative sense.  The test indicates the presence of peptide bonds, which are the basis for the formation of proteins.  The classic test for the presence of peptide bonds is the presence of a purple color, as is shown here.  A superficial examination of the literature will indicate that the Biuret Test can only be used to detect peptides with three or bond bonds present; i.e., a tripeptide or larger, and this will result in the purplish color shown.  A dipeptide bond, however, has only two peptides that are joined together.  A deeper search in the literature will reveal that the Biuret Test will indeed respond to dipeptide bonds, but that there will be a shift to a longer wavelength in the spectrum (ie., a shift towards the blue).  With careful examination, this shift in wavelength can be observed in a spectral analysis, and it is critical in determining whether a dipeptide or a longer peptide form is in existence.

purple drink

Aspartame
A reference and control spectral plot of Aspartame, a dipeptide.

3. The next level of confirmation is to establish that a dipeptide is present in the compound using the methods of spectral analysis in combination with the Biuret Test.  An early observation made with the Biuret Test applied to the eluate was that the color observed was shifted toward the blue end of the spectrum compared to the classical Biuret Test.

It therefore became necessary to establish a dipeptide control case using spectral analysis.  Aspartame serves as such a control, as it is a dipeptide (meaning two peptides joined together).  The distinguishing case of the shift in wavelength as referred to in the more exhaustive literature is therefore proven with the reference case shown here.  A tripeptide or larger will show the peak at approximately 600 nm; the dipeptide will show the peak shifted to approximately 640 nm.  The rise toward 340 nm is also a distinguishing characteristic.

The match in the spectrums between the control and the eluate makes the strong case that a dipeptide is a core constituent of the proteinaceous complex under examination.

chromatography column eluate
A spectral plot of the chromatography column eluate.  The correspondence and match with the reference dipeptide spectrum above is apparent.

4. The next level of confirmation for the existence of the proteinaceous complex is with the use of ninhydrin.  Ninhydrin is a chemical substance that reacts distinctively in the presence of amino acids and heat.  Amino acids turn a characteristic purple and or brownish color in the presence of ninhydrin and heat.  The use of ninhydrin is one of the classical means for fingerprint detection in forensic science.  The ninhydrin test here proves the existence of amino acids as further confirmation of the dipeptide assessment reached previously through spectral analysis.

ninhydrin test
A ninhydrin test on aspartame as a control to the left and the same test on the proteinaceous eluate on the right.  Both tests are clearly positive for the presence of amino acids.

 

 reference set of amino acids
A reference set of amino acids subjected to a ninhydrin test in solution.  Unique and identifiable color spectrums at a specific pH result for each amino acid. pH of the solution is an important variable in the color of the solutions that results.  Number 7 in the set is aspartame in solution and number 8 is the solution under examination.  The visual agreement with cysteine (number 2) is apparent; spectral analysis confirms this assessment.

5,6. A reference set of amino acids solutions subjected to ninhydrin and heat is created.  Unique and identifiable colors spectrums are created for each amino acid.  Spectral analysis can now be used to create a set of reference spectrums for the amino acids.   Such reference spectrums were created for argenine, cysteine, glutamine, glyceine, histidine, lysine.  A reference spectrum was also created for aspartame; a particular dipeptide.

 

7,8. The first test tube in this set is the proteinaceous eluate.  The second test tube is the eluate subjected to the Biuret Test; proving the existence of the dipeptide form (passes spectral analysis test in addition).  The third test tube is the Biuret Test case subjected to N-Acetyl cysteine.  At this point, the Biuret Test turns clear, indicating that the dipeptide bonds have been broken.  When the resulting clear solution is tested for iron in the ferric state (II) the test is positive.  

This is an important observation and chemical test result that will be discussed in greater detail in a later report. In summary, however, this test demonstrates the reduction of the dipeptide bonds and the release of free iron in the ferrous state (II).    

It will also subsequently be demonstrated that the amino acids contained within the dipeptide are now in their free form.

otter pops

9. The last test to be briefly presented demonstrates the presence of the cysteine amino acid within the complex.  When the eluate is subjected to N-Acetyl cysteine, the dipeptide bonds are broken and the iron is released in its free state.  The amino acids, now in their free stated, can be subjected to ninhydrin and heat and a spectrum developed.  It will be found that the resulting spectrum will match that of cysteine.  This rather complex combination of tests and events will lead to the assessment presented earlier that the protein consists of a metalloid dipeptide complex involving iron in the Fe (III) state combined with cysteine amino acids.

reference spectrum for cysteine
A reference spectrum for cysteine after being subjected to ninhydrin and heat.

a case of the eluate being subject to the Biuret Test

On the left is a case of the eluate being subject to the Biuret Test (originally blue-purple), then subject to the addition of NAC.  The dipeptide bonds are broken and the solution turns clear.  On the right, the solution from the previous step is subject to ninhydrin and heat.  This produces the yellowish color in the tube to the right.  The spectrum of this case is presented at the lower left, and matches that of the reference spectrum for cysteine.  NAC with ninhydrin and heat by itself produces no such color reaction or spectrum.  This result solidifies the assessment of the proteinaceous nature being a complex of both cysteine and iron.

spectrum of the proteinaceous complex

The spectrum of the proteinaceous complex after being subjected to the Biuret Test, N-acetyl cysteine, ninhydrin and heat.  N-acetyl cysteine breaks the dipeptide bonds which releases the iron and the amino acids into their free from.  When heated with ninhydrin, the spectrum of the amino acid will match that of cysteine as shown above. The spectrum must be taken immediately after removal from the hot water bath with ninhydrin.

Clifford E Carnicom
Born Clifford Bruce Stewart
Jan 19 1953

MORGELLONS AND RECENT FINDINGS

MORGELLONS  AND RECENT FINDINGS:

PART I : MORGELLONS : A REVERSAL STRATEGY

PART II : PROTEINACEOUS FORM IDENTIFIED

PART III : DIMORPHISM, SYMBIOSIS OR DESIGN

PART IV: MAGNETIC PROPERTIES OF THE GROWTH FORMS

PART V : DNA EXTRACTION

PART VI: THE SERBIAN SAMPLE

PART VII : COLUMN CHROMATOGRAPY

PART VIII : CONFERENCE VIDEO EDITING PROJECT

PART IX : CULTURE GROWTH RATE IMPROVED

PART X : ELECTROPHORESIS PROCESS BEGINSPART

XI : ANOTHER POSITIVE TEST METHOD FOR IRON (Fe+3) IN THE CULTURE

IN PROGRESS
Estimated Completion Date : Can Not Be Estimated At This Time

Clifford E Carnicom
Jan 2012

Note: I am not offering any medical advice or diagnosis with the presentation of this information. I am acting solely as an independent researcher providing the results of extended observation and analysis of unusual biological conditions that are evident.  Each individual must work with their own health professional to establish any appropriate course of action and any health related comments in this paper are solely for informational purposes and they are from my own perspective.

 

PART I : MORGELLONS : A REVERSAL STRATEGY (Dec. 18, 2011)

A viable and tangible strategy to disrupt the growth process of the Morgellons condition, as it exists within the culture form that has been developed, has been established.  This strategy involves the breakdown of certain chemical bonds within an identified proteinaceous complex in a manner that is not harmful to the human body.  The reduction strategy also includes the release of iron that is held within the proteinacous complex in a chelated form.  This strategy has been established with confidence and a repetition of results.  The current work will be applied next directly to oral human samples.  Much time, energy and resources will be required to further investigate, verify and apply this strategy. The preliminary results and the theories are promising at this stage.

biuret iron

To be continued

protein graph

To be continued

PART II: PROTEINACOUS FORM IDENTIFIED

A note to the staff of the Institute tonight (Dec. 2, 2011); this will give some idea as to some of the work in progress…


The existence of a protein within the culture growths has now been established with confidence tonight. I had to do work to eliminate questions of potential contaminants that might have distorted the results. It is also a process of much patience with chromatography, literally drip by drip over many days for each test that is set up. It has taken about 1 1/2 to 2 months to get to this point.

Existence of a protein is eventually of equal importance as that of the iron work. We now have iron and the protein as two primary and identified constituents. This work will raise more questions that it answers, but we need to live with this for now until future means and equipment and methods work their way in. One more reliable way of putting a stop to this fellow is to truly understand the biochemistry and the life cycle of growth; there is then a better chance of interfering with that cycle in a known manner.

The existence of a protein means there is DNA behind it. As you can imagine, the work has actually just begun if we can get these means. Next questions would be what type of protein, what is the function of the protein(s), sequencing of the proteins, etc. Right along with it would be the isolation of DNA, electrophoresis work, etc.  An infra-red spectrophotometer would be a very useful piece of equipment for us on an ongoing basis – we are having to work very hard to get certain results that would be more apparent with the right equipment.

I may put this comment on the paper to get the process started, otherwise I have so many to write I will never get to any of them at the current rate…

Clifford

 A positive Biuret protein test result

A positive Biuret protein test result using a separation of elute from the chromatography column. The sample material is based upon a culture from oral filaments.  The original extraction from the chromatography column is to the left; the positive Biuret result for the existence of a protein is shown on the right with the purple color.  Successful separation on the column has been achieved using various combinations of solvents in combination with a stationary phase

A positive Biuret test result using whey

A positive Biuret test result using whey (lactoferrin) protein for control purposes.  A positive test results in the purplish color shown above.  The Biuret test depends on a copper complex that forms between the protein (peptide bonds) and copper sulfate and an alkaline solution, such as sodium hydroxide.

PART III: DIMORPHISM, SYMBIOSIS OR DESIGN

The morphology, metabolism and life cycle of the “Morgellons” organism, as defined by this researcher, is increasingly being understood.  There are now three scenarios that can be provided that encompass the majority of the understanding that has been achieved.  

The first of these examines a similarity of form, at least in part, to a dimorphic fungal-like organism.  

The second considers the joint existence of bacterial-like and fungal-like organisms in a symbiotic relationship.  

The last raises the spectre of a genetically created or designed organism.  

Each of these scenarios has certain strengths, weaknesses and probabilities of occurrence.  There can also be a degree of overlap between these alternative interpretations.  This paper will discuss what has been discovered, within these three scenarios,  that helps us to potentially define the nature of this unusual organism.

morphology 1

morphology 2

morphology 3

morphology 4

morphology 5

morphology 6

morphology 7

morphology 8

morphology 9

morphology 10

morphology 11

morphology 12

morphology 13

morphology 12

morphology 13

PART IV: MAGNETIC (ELECTROMAGNETIC) PROPERTIES OF THE GROWTH FORMS:

The magnetic (and consequently, the electromagnetic) properties of the primary Morgellons growth form are now proven in a direct fashion.  The video segments below show the response of both the culture derived form and the oral sample to a strong magnetic field.  These demonstrations will call into consideration each of the papers written on the subject of electromagnetics by this researcher.  One such topic will be the extended research that has been done that reveals the ambient presence of unaccounted Extremely Low Frequency (ELF) energy over a testing period of several years.  The human electromagnetic system operates primarily within the ELF portion of the electromagnetic spectrum.  The sensitivity and response of the Morgellons growth form to the electromagnetic spectrum is another of the many primary fields of research that requires funding, resources and skilled personnel to complete.  The identified presence of iron and ferromagnetic compounds within the growth forms establishes the basis of this future research, along with the direct demonstration of the magnetic response shown below:


To be continued.


PART V: DNA EXTRACTION

dna 1 dna 2 dna 3

To be continued.


PART VI: THE SERBIAN SAMPLE

To be continued.

serbia 1 serbia 2
serbia 3
serbia 4 serbia 5
serbia 6 serbia 7
serbia 8

PART VII: COLUMN CHROMATOGRAPHY

To be continued.

column 1

column 2

 

PART VIII : CONFERENCE VIDEO EDITING PROJECT

 

To be continued.

PART IX : CULTURE GROWTH RATE IMPROVED

To be continued.

X : ELECTROPHORESIS PROCESS BEGINS

ELECTROPHORESIS 1

Starch Gel Electrophoresis Applied to Proteinacous Samples : Initial Tests Underway

ELECTROPHORESIS 2

ELECTROPHORESIS 3

Starch Gel Electrophoresis : Trial Runs of Test Dyes and Blood Sample.   Left photograph shows methylene blue dye migration towards the negative terminal. Arrows on right photograph depict origins of placement.  Blood sample shows both positive and negative charged protein component separation at lower portion of right photograph.  Eosin test case on upper left of right photograph; migration toward positive terminal  Methods remain under development; no successful separation of presumed culture based proteinacous component at this time.

To be continued.

XI :ANOTHER POSITIVE TEST METHOD FOR FERRIC IRON (Fe3+) IN THE CULTURE

Another test method has been developed to detect and establish the presence of iron in the Fe3+ state within the culture growth that is based upon the oral samples.  The test is positive.  The further significance of this test is that it has been applied directly to the proteinaceous complex that has been extracted from the culture with the use of column chromatography.  This further substantiates the case that the proteinaceous complex itself contains iron in the ferric state and that this iron is bound to certain amino acids that are under examination as candidates.   It will be possible to determine the concentration of the iron within the proteinaceous complex through spectrometry.  The test is based upon the use of ammonium thioglycolate.

Clifford E Carnicom
(born Clifford Bruce Stewart Jan 19 1953)