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A Guest Posting: Ten Questions for Alan Adler by Kelly Kearse

10+ Questions that I would ask Alan Adler

In the light of several recent discussions involving various Shroud investigators, I decided to jot down several specific questions that I would ask Dr. Alan Adler if given the opportunity to have a face to face discussion with him.  I tried to limit my questions to 10 main points of interest. Of course, Adler "is not here to defend himself", but he doesn’t have to-at least not to me.  The intent of this posting is not to represent a type of cross-examination, far from it-this posting merely models a focused discussion with specific questions from someone who is seeking to increase their understanding. These are the questions I would have. Yours, of course, may be different.  And the answer to one question may naturally spawn three more.  But that’s how discussions move forward.  If you’re old enough to remember the lines, "I asked Bobby Dylan.  I asked the Beatles…"; well, in this discussion exercise, I am asking Alan Adler-or at least pretending to. Of course, others may eavesdrop on this imaginary conversation and contribute as they choose-that of course, is the point.  

First, allow me to say that it is truly an honor & privilege to have this opportunity. I have followed your work with great interest-my background is in immunology & cell biology, the blood typing studies are what first seriously caught my attention about the Shroud. I am not a blood ‘specialist’; my questions may appear somewhat detailed at times, and at others, rather naïve. I hope that is okay. I appreciate this opportunity and thank you again for your time.

1. In your article “The Origin and Nature of Blood on the Turin Shroud”, published in 1986, you wrote: “The next test we did was to take micro-spectrum photometry on the non-birefringent red-coated fibrils from the Shroud. It was obvious that the spectrum it produced did not match the spectrum of methemoglobin, at least not given in the standard references, which is a solution spectrum of blood. This is one of the problems in trying to look in the literature for references to compare the results to.” It is somewhat surprising that the literature is rather limited relative to the spectra studies of blood that is not in solution. Besides the oxidation of hemoglobin to methemoglobin in dried (aged) blood, what are the other major differences in the spectra of blood in solution versus dried blood? Also, what are the major differences in the spectra of freshly dried blood (2-3 days old) versus blood that is years, even several decades (or more) old?

2. In the same article, you mention that “In a film of hemoglobin there is a conformational change; it no longer remains in the “met” form but goes to the para-hemic form. Can you distinguish for me, exactly what the difference is between the structure of the para-hemic form and the met form? Is the para-hemic form an opened ring form of hemoglobin that has begun the breakdown process, or does this refer to the position of an attached group shifting its location on the ring (ortho, meta, para like we learned in organic chemistry years ago)? Or is the term “para” in reference to paramagnetic, a species that contains unpaired electrons? Forgive me if this question is very basic, but when I search the terms on the internet, most of the references that come up are the sentences from your article. I’ve also thumbed through various physiology and physical chemistry texts but so far, have struck out. Can you draw me a diagram or give me a reference that has a picture of the two structures? Also, what drives this conformational change-does this result from the dehydration of the blood as it dries into a film?

3. In the same article, it is said that “It is known now that there is a certain species which will spontaneously go to the para-hemic form if there is not enough turnover in the spleen and the liver to process the blood fast enough”. This sounds like a relatively recent observation. The word that confuses me the most here is “spontaneously”, is this a type of isomerization that is occurring here? Is there a specific enzyme that catalyzes the change? Is this independent of the oxidation state of hemoglobin?

4. Also in the 1986 article, it states “We found a spectrum that was characteristic of only one known group of compounds-the so-called high-spin, high-iron porphyrins. What we were seeing is the breakdown products of hemoglobin-bilirubin and biliverdin. There is an extraordinary high bilirubin count, almost as high as the methemoglobin” Just to clarify, this is methemoglobin (deoxygenated hemoglobin), all or most of which exists in the para-hemic form, not the typical met-form? Also, what is the relative proportion of bilirubin and biliverdin that is observed?

5. What exactly is meant by “high-iron” porphryins? High spin refers to the electron configuration, that this conformation has the maximum number of unpaired electrons available, but what does the term “high-iron” denote? Is this in reference to Fe-containing porphyrins to distinguish them from other porphyrins (which contain a ligand other than Fe being bound), or is there another significance?

6. In the 1986 article, you state “You now mix bilirubin which is yellow-orange with methemoglobin in its para-hemic form which is an orangey-brown and you get blood which has a red color. In fact, we have been able to simulate this spectrum in the laboratory.” Relatedly, in the 1998 Shroud Symposium held in Dallas, TX, in the article “Further Spectroscopic Investigations of Samples of the Shroud of Turin” it says “A simulation of such a traumatic blood exudate prepared from laboratory chemicals as a control matches the appearance and properties of this class of test objects. A traumatic clot exudate simulacrum was approximated by mixing 3 drops of blood (finger stick) with three drops of a bilirubin/human albumin diagnostic standard (Sigma Chemical Co.). Dried whole blood, bilirubin, and human hemoglobin samples were employed as controls.” Exactly how much exogenous bilirubin was added relative to the hemoglobin present in the finger stick? How does this compare to what would be considered normal levels? In this article (and others) there is no mention of specific amounts-[I have looked through the current Sigma catalog, but was unable to find this particular product-may have been discontinued]. Also, was the majority of hemoglobin used in these experiments (finger stick) in the deoxygenated form? Finally, did you ever spot such samples onto cloth (linen) and evaluate if the red color persisted over time?

7. In whole blood, the relative amount of bilirubin present is normalized per blood unit volume, making it straightforward to compare levels between individuals. In dried bloodstains, how does one accurately quantitate or even approximate the relative level of bilirubin present as volume cannot be used for normalization? Several spectroscopy and forensic “experts” I have e-mailed or talked to on the phone have acknowledged that spectroscopy of dried samples is semi-quantitative at best. I have run across a few presentations suggesting that the samples may be weighed and then normalized relative to Fe content, but such techniques involve larger volumes of blood than would be present in tape lift samples or individuals threads, and appear to be in the early stages of development. It is unclear even today if such methods would be sensitive enough to apply to the relative small amounts of blood in your analysis. No specific values or approximate ranges for the relative amount of bilirubin present were ever given in your articles-can accurate values be obtained from the techniques that were in use during these studies? If so, what are the estimated values?

8. In the 1980 article “Blood on the Shroud of Turin”, you state that in reference to the spectra of the Shroud fibrils that “the high degree of scattering from these solid samples makes the visible band shape features less distinct and does produce peak shifts from the solutions spectra. Therefore this identification is much less positive than desired.”

In the 1998 Shroud meeting in Dallas, TX you note that “Hemoglobin exists in lots of states and it’s a real problem on the Shroud to know what some of these states are.” In communicating with several specialists in heme spectroscopy about the spectral profiles (without indicating they were of the Shroud and cropping all identifiable labels on the Figures), the opinion was voiced that “it is impossible to really say what species are present there-the background is too high and the peaks are poorly resolved.” Different scientists have different opinions & viewpoints-I am certainly confident in your ability to identify the sample as blood and in the characterization of blood components, but it sounds as though there are still some large unknowns as to exactly what species might exist. Is it possible for us to look at the spectra of a Shroud sample together (and also a blood simulacra sample) and for you to take me through this, from left to right, peak by peak, and point out the probable identity of everything that is represented there? Is the resolution of biliverdin, bilirubin or other breakdown products more straightforward than various oxidized species of hemoglobin that may be present?

9. In your 1993 article, “Conservation on the Shroud of Turin” you emphasize that “bilirubin can be readily and quickly photodecomposed under a variety of conditions”. Given the relative instability of bilirubin, how do you account for its preservation on the Shroud over a relatively long period of time? Could this be due to aggregation of (high concentrations of) bilirubin in dried bloodstains as opposed to bilirubin in solution? Or some type of chemical bonding/association between bilirubin and the cloth? Thoughts?

10. Growing up, what first stimulated your interest in science? Were you always interested in pursuing a scientific career?

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