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Monday, April 15, 2013

Fossils and Fossil Rocks KILL OFF Evolution - With Ian Juby also Part Ten, the rest of the story - Real Flesh and Blood Remains!

I love Ian Juby videos!!!  Search for Wazooloo on YouTube to find him or click here!

Piltdown Superman's joke near the end is funny by the way...but Ian's information about the geological column and the lies told by Darwinists is not.   Lies, propaganda, mythology, censorship, banning, blackballing...these are the ways of the Darwinist.  Only a minority of them either even consider any other explanation and the majority of those who do see there is a competing viewpoint are dedicated to keep this information from the publc.

Look, if gasoline costs $3.75 in your area and all the gas stations advertise about the same rate, what happens if a new station a couple of miles down the road begins selling it for 59 cents a gallon?  Would the other gas stations even admit it?  Nope.   They would pass out rumors that the gas at that station is bad, contaminated with water, illegally mixed, dangerous to your engine, anything they could think of to keep you from trying it out because once you paid 59 cents for gas you would not pay the high prices again!!!

Same with Darwinism.   Once you realize that the evidence supports Creation by God, you are going to realize how absurd Darwinism really is and dump it entirely as a myth.  So Darwinists do what they can to keep people from finding out what Creation Science teaches and also finding out about all the lies and deceptively presented faked and altered pictures and charts and even modified fossils!!!

 I will leave you with one last observation.  There is a common saying among scientist that "finding the head of a dinosaur is like finding a needle in a haystack." 2   This is to say that the greatest majority of dinosaur skeletons found have no head attached to their bodies.  There are actually only a dozen or so complete dinosaur skeletons in the entire world.  Many more dinosaur skeletons than this have been found of course, but they are not complete. Often they are missing their heads.  Why would a dinosaur loose its head if it died a simple death and just fell over on the ground to be buried?  Even scientists admit openly that it appears like most dinosaurs were washed into their current locations by heavy currents.2   A head is not as well attached to the rest of the body as other limbs.  A catastrophic flood could be the reason that there are so many headless dinosaurs around. 

Dinosaur Soft Tissues and Blood

"The lab filled with murmurs of amazement, for I had focused on something inside the vessels that none of us had ever noticed before: tiny round objects, translucent red with a dark center. Then a colleague took one look at them and shouted, 'You've got red blood cells. You've got red blood cells!'.  It was exactly like looking at a slice of modern bone. But, of course, I couldn't believe it. I said to the lab technician: 'The bones, after all, are 65 million years old. How could blood cells survive that long?'" 10,11,50         
This account was given by Mary Schweitzer, a PhD student at the time, from Montana State University.  A well preserved Tyrannosaurus Rex skeleton had been found in 1990 and brought for analysis to Montana State University.  During microscopic examination of the fossilized remains, it was noted that some portions of the long bones had not mineralized, but were in fact original bone.  Upon closer examination it was noted that within the vascular system of this bone were what appeared to be red blood cells (note retained nucleus in the center of the apparent RBCs and the fact that reptiles and bird generally retain the RBC nucleus while mammals, like humans, do not). 50 Of course, this did not seem possible since the survival of intact red blood cells for some 65-million years seems very unlikely if not downright impossible.  
Further testing of these cells was done to attempt to disprove the notion that they could possibly be red blood cells.  Several analytical techniques were used to characterize the material to include nuclear magnetic resonance (NMR), Raman resonance and Raman spectroscopy (RR) and electron spin resonance (ESR).  These techniques did identify the presence of heme group molecules ranging in size from between 5,000 and 30,000 daltons (between 35 to over 200 amino acids in size), but the detection limits of these methods were not able to rule-out or rule-in the presence of hemoglobin or myoglobin proteins due to the small amount of specimen available.   So, Schweitzer and her team decided to use a more sensitive detection method to detect certain very specific types of proteins. They used the immune system of rats.  They injected some of the T. rex extract into laboratory rats to see if these rats would mount an immune response to the foreign T. rex material.  And, the rats did mount a very specific immune response against hemoglobin.  This immune response was not just against hemoglobin in general, but against certain types of hemoglobin.42 The reaction was strongest against pigeon and rabbit hemoglobin with a weak reaction against turkey hemoglobin, but there was no reaction against snake hemoglobin.  The specificity of these reactions were further confirmed by the lack of reactivity with plant and sandstone extracts. 
This is significant since many previous real time studies with protein decay suggest that sizable portions of protein sequences do not remain intact beyond a few tens of thousands of years at best (Fossils, Protein and DNA). Proteins and DNA usually decay very rapidly. Therefore, it would be quite something indeed to find significantly intact hemoglobin after tens of millions of years. Some have even suggested that significantly intact proteins would indicate that such fossils are not in fact tens of millions of years old, but were in fact recently buried within only a few tens of thousands of years at most. 
Consider the conclusions that Schweitzer and her team made concerning these findings: 

"The production of antibodies specific for hemoglobin in two rats injected with the trabecular extract is striking evidence for the presence of hemoglobin-derived peptides in the bone extract. . . That the antisera did not react with snake hemoglobin shows that the reactivity is specific and not artifact. . . When considered as a whole, the results support the hypothesis that heme prosthetic groups and hemoglobin fragments were preserved in the tissues of the Late Cretaceous dinosaur skeleton." 42

These results are quite interesting since they indicate a very specific immune response, not just against hemoglobin, but certain types of hemoglobin molecules. Note again that the antibodies formed did not react against snake hemoglobin indicating that the antibody reactivity was "specific and not artifact." The question is, how much of the original T. rex hemoglobin molecule would need to be intact to elicit such a specific immune response in the laboratory rats?
Schweitzer goes on to suggest that "Immunogenicity is not dependent on fully intact protein, and even very small peptides are immunogenic when complexed with larger organic molecules . . . even after extensive degradation has occurred."42 But how extensively, roughly, could the hemoglobin molecules have degraded and yet retain their ability to elicit a fairly strong and quite specific immune reaction in laboratory rats?  In order to obtain such strongly specific immunogenicity it would seem that a significant percentage of the globin portion of the hemoglobin molecule would need to be intact in at least some of the extracted specimen. In fact, larger molecules were indeed present. Schweitzer proved that there were heme-containing molecules ranging from at least 5,000 to 30,000da in size, and maybe even larger. But, how could a protein of any significant size large enough to elicit an immune response to begin with, as well as a specific immune response observed in this case, be maintained over the course of 65 million years?  One might very reasonably conclude that natural decay, over this amount of time, would completely destroy the ability of hemoglobin or the required larger fragments of degraded hemoglobin from being antigenic much less so specifically antigenic.
The explanation for this phenomenon, given later by Dr. Horner (Schweitzer's boss) and even Schweitzer herself, was that the tougher heme molecule survived the 65 million years with maybe three or four amino acids of the original globin molecules attached to it.  Consider the following statement Schweitzer made in a response to an inquiry by Dr. Jack Debaun:

"But the heme itself is too small to be immunogenic [only about 652 daltons].  We believe that there were possibly 3-4 amino acids from the original protein attached to the heme, and that was what may have spiked the immune response." 43

Now, it just seems quite unlikely that just 3 or 4 amino acids stuck onto a heme group is going to give rise to an immune response at all not to mention a specific immune response for a certain type of hemoglobin as was found in this case (Note that a fully formed globin molecule ranges from 141 to 146 amino acids in length with specific folding characteristics that make up various antigenic "epitopes" that antibodies detect). As far as I have been able to tell, the degree of immune response specificity noted by Schweitzer et al. has never been realized in any confirming experiment with so few hemoglobin amino acids stuck to a heme group (just over 1,000da in size). Even if such an experiment were successful, it certainly doesn't seem like a very likely explanation in this case.  
There are several reasons why I feel this way.  For one thing, a certain minimum antigen size is required before it can elicit an immune response regardless of its structure. The most potent immunogens are macromolecular proteins with molecular weights greater than 100,000da (~740aa - Note: the average amino acid weighs ~135da).  Substances weighing less than 10,000da (~75aa) are only weakly immunogenic, and those foreign proteins/antigens weighing less than 1,000da (~7aa) are usually completely non-immunogenic. Homopolymers (repeats of the same amino acid) are pretty much non-immunogenic regardless of size.  Co-polymers of glutamic acid and lysine must be ~35,000da (~250aa) to be immunogenic.  It seems then that, in general, immunogenicity increases with structural complexity.  Also, aromatic amino acids, such as tyrosine or phenylalanine, contribute much more to immunogenicity than do non-aromatic amino acids.  For example, the addition of tyrosine to a co-polymer made up of glutamate and lysine reduces the size limitation to ~15,000da (~100aa) and adding tyrosine and phenylalanine together reduces the minimum to 4,000da (~30aa).  Also, it is all four levels of protein structure (1o, 2o, 3o, & 4o) that influence immunogenicity - not just a short linear sequence of amino acids.44-47
Of course, a rather specific immune response can be elicited by relatively few amino acids as part of an epitope on a larger protein molecule, but they usually are not immunogenic without first being part of a larger molecule (i.e., "complexed" to a larger molecule before being introduced to the immune competent host).  Also, antigenic epitopes are not usually sequential in nature but are assembled by protein folding (i.e., bringing together amino acids that are widely separated on the protein chain).  This means that a rather large portion of the original molecule usually needs to be intact in order for most epitopes to remain intact.  Epitopes with definite three-dimensional shapes and charged amino acids are particularly well recognized by antibodies. The average epitope probably involves about 7 to 15 contact amino acid residues and a few of these may be critical to the epitope's specificity and the avidity of the antibody-antigen reaction.44-47  But, in order to make an epitope antigenic, it must be processed first.
Antigen presenting cells (APCs) like macrophages, dendritic cells, and even B-cells are responsible for antigen processing and the presentation of epitopes/antigens to the T-cells.  T-cells do not recognize the initial foreign antigen directly.  They only recognize processed parts of antigens, usually consisting of no more than 15 or so amino acids, presented to them by APCs in association with MHC (major histocompatibility) molecules.  So, in order to activate T-cells (required for cellular immunity and very helpful in humoral immunity), the foreign antigen must first be recognized as "foreign" by the APC cells.  This initial APC recognition requires more than just a handful of amino acids floating around or else there would be complete meltdown of the immune system.  In fact, generally speaking, molecules with a molecular weight less than 10,000da (~75aa) are only weakly immunogenic when picked up by APC cells.  Significant potency usually requires antigens to be rather large at over 100,000da (~750aa), or at least above 5,000da (~35aa).48,49 
Given all this, it seems quite difficult for me to imagine how "3 or 4" amino acids stuck to a heme group could elicit an immune response in the first place, not to mention a specific immune response.  Recall that the heme molecule, by itself, only has a molecular weight of around 652da.  To make a strong as well as specific immunogen (such as the immunity developed in rats exposed to T. rex extract in this case) one might expect the immunogenic hemoglobin molecules to be at least 5,000 to 10,000da (~35 to 75aa or so) in size.44-47 Certainly then, a heme group with 3 or 4 amino acids attached to it (just over 1,000da) would not seem to give rise to such an immune response (specific to a certain type of hemoglobin) observed by Schweitzer et al. in rats exposed to T. rex bony extract. 
There are several common arguments used to try and explain these apparent difficulties. One argument is that very small degraded fragments of hemoglobin molecules (3 or 4 amino acids in size) reattached themselves to each other to form new larger molecules with sufficient size to be immunogenic. The problem here is that the rearrangement of so many covalent bonds over the course of some 65 million years would seem to affect not only the inter-amino acid bonds, but the intra-amino acid bonds as well. Of course, such a degree of rearrangement would destroy antigenic epitope specificity. Note also that the heme molecule itself is not bound by covalent bonds to the globin portion of the hemoglobin molecule. It is held in place in a crevice of the globin molecule by many non-covalent bonds that are individually much weaker than the covalent bonds that hold the amino acids together. If the covalent bonds were so commonly broken over time so as to leave only very small chains of 3 or 4 amino acids from the original globin molecule intact, how was the much weaker non-covalent bond between the heme group and a small chain of only 3 or 4 amino acids maintained? It would seem that as the protecting crevice surrounding the heme group was degraded to any significant degree that the non-covalent bonds holding the heme group molecule in place would not have lasted very long. The heme group would have been lost long before the much stronger covalent bonds between amino acids in chains much longer than 3 or 4 amino acids would have been broken.  
Another argument is sometimes used that Schweitzer failed to identify any specific size of hemoglobin fragment by gel electrophoresis.  What happened is that the electrophoretic pattern observed by Schweitzer was a diffuse or smeared pattern.  This means that there were no discrete clusters of proteins that were the same size.  Certainly, this is only to be expected since a wide range of protein sizes would be formed after an extended period of degradation.   The fact of the matter is that hemoglobin fragments ranging between 30 and 200 amino acids in size where definitely present in the T. rex extract (per NMR analysis filtering) and that these molecules were most likely intact fragments of the original T. rex hemoglobin molecules and not reformed molecules made up of tiny fragments.42
 If this is not already enough, Schweitzer recently made an even more startling discovery.  About three years ago (2002) she and her team had to divide a very large T. rex thigh bone in order to transport it on a helicopter. When the bone was opened flexible soft tissue "meat" was found inside. This is incredible because this bone was supposed to be some 68 million years old. Microscopic examination revealed fine delicate blood vessels with what appear to be intact red blood cells and other type of cells like osteocytes - which are bone forming cells. These vessels were still soft, translucent, and flexible. Subsequent examination of other previously excavated T. rex bones from this and other areas have also shown non-fossilized soft tissue preservation in most instances.54   
This find calls into question not only the nature of the fossilization process, but also the age of these fossils. How such soft tissue preservation and detail could be realized after 68 million years is more than miraculous - - It is unbelievable! Schweitzer herself comments that, "We may not really know as much about how fossils are preserved as we think." 54  Now, if that is not an understatement I'm not sure what is.
So, it seems rather clear, despite the objections of many evolutionists, to include Schweitzer herself, that a 1,000da molecule would elicit an extremely weak response at best and would not necessarily elicit a specific response to a certain type of hemoglobin molecule since surface epitopes are generally more specific in their antigenic nature than are buried epitopes (i.e., heme is somewhat hidden within a cleft of the hemoglobin molecule so 3 or 4 amino acids attached to it would also be somewhat hidden). How then is it remotely logical to suggest that a molecule weighing just over 1,000da (a heme group plus 3 or 4 amino acids) could elicit such a strong as well as specific immune response as Schweitzer et al. observed?  In light of the additional recent finds of even more striking soft tissue and blood cell preservation, it seems much more likely that such an immune response so specific for certain types of hemoglobin could only be elicited by a larger portion of intact hemoglobin than many scientists seem to even consider.  Of course, one can't really blame them because explaining how delicate soft tissue vessels (with obvious red blood cells inside containing relatively large portions of hemoglobin molecules) could remain intact for over 65 million years seems just a little bit difficult. 
All of this is a rather mute point, of course, in light of the fact that T. rex collagen has been subsequently sequenced.

       "I mean can you imagine pulling a bone out the ground after 68 million years and then getting intact protein sequences?" said John Asara of Beth Israel Deaconess Medical Center and Harvard Medical School, lead author of one of the studies. "That's just mind boggling how much preservation there is in these bones."
       The new finding will be viewed skeptically, admitted one of the researchers involved in the two studies. "It's very, very, very controversial because most people have gone on record saying there's an absolute time limit to anything that's protein or DNA," said Mary Schweitzer, a molecular paleontologist at North Carolina State University.
       Matthew Carrano, a dinosaur curator at the Smithsonian Institution in Washington, D.C., who was not involved in either study, said the protein findings are robust. "Here are the pieces of the protein. If you're going to refute this you have to explain how these pieces got in there," Carrano said in a telephone interview. "It's not another molecule mimicking the protein and giving off a similar signal. This is the actual sequence." 99
Of course, despite this surprising turn of events, scientists do not question the notion that the dinosaur bones really are tens of millions of years old.  They still assume the long ages and evolutionary relationship that they assumed before - as per the following passages:

       A comparison by Asara's team of the amino-acid sequence from the T. rex collagen to a database of existing sequences from modern species showed it shared a remarkable similarity to that of chickens. Amino acids are the molecular building blocks of proteins; there are 20 of them used by organisms to build proteins, and their precise order is determined by instructions found in DNA.
       "I'm grateful that he was able to get the [amino acid] sequences out. That's the Holy Grail," Schweitzer told LiveScience. . .  Until now, family trees have been constructed from the shapes of bones and teeth, a not-always-reliable technique."
       This finding supports the idea that chickens and T. rex share an evolutionary link and bolsters previous research showing that birds evolved from dinosaurs and that birds are living dinosaurs.
       "Here we have a real molecule from a real dinosaur, and it's much more similar to a bird than it is to anything else," Carrano said. 99
Mary Schweitzer's 60 Minutes Interview

Such finds are much more consistent with a fairly recent catastrophic burial within just a few thousand years of time. Non-catastrophic burial would allow for rapid biodegradation of such delicate soft tissues. Time itself destroys soft tissues as well as DNA and proteins in short order.  Current real-time observations suggest that bio-proteins could not remain intact more than a few tens of thousands of years - 100,000 years at the very outside limit of protein decay.  The fact that such proteins are found, intact, in bones supposedly older than 65 million years is simply inconsistent with such an assumed age - by a few orders of magnitude.


So, where does the evidence put us?  What position seems most reasonable?  What theory answers the most questions?  Do fossils and the geologic column that contains them represent millions of years of slow sedimentation or do they reveal a time of huge catastrophe and rapid deposition, death, and burial on a global scale? (Back to Top)

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