The idea of dinosaur hemoglobin comes from this paper:
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=21042
The Abstract reads:
"Six independent lines of evidence point to the existence of heme-containing compounds and/or hemoglobin breakdown products in extracts of trabecular tissues of the large theropod dinosaur
Tyrannosaurus rex. These include signatures from nuclear magnetic resonance and electron spin resonance that indicate the presence of a paramagnetic compound consistent with heme. In addition, UV/visible spectroscopy and high performance liquid chromatography data are consistent with the Soret absorbance characteristic of this molecule. Resonance Raman profiles are also consistent with a modified heme structure. Finally, when dinosaurian tissues were extracted for protein fragments and were used to immunize rats, the resulting antisera reacted positively with purified avian and mammalian hemoglobins. The most parsimonious explanation of this evidence is the presence of blood-derived hemoglobin compounds preserved in the dinosaurian tissues."
Now, the Abstract makes clear that we are dealing with
fragments of the protein.
Now, how can these fragments be preserved for millions of years? Here's the answer in the paper, but apparently the creationist sites never mentioned it:
"Most erythrocytes undergo hemolysis when the organism dies. Hemoglobin is released with a resultant red discoloration of surrounding bony tissues (
22). However, under the anoxic conditions that prevail deep in the endosteal tissues of massive animals (
28), hemoglobin molecules may be protected from early stages of oxidative degradation. The proteins may then become complexed with apatite, the mineral phase of bone matrix. This association may well be a prerequisite for the survival of biomolecular compounds across geological time (
29,
30). Protein and other organic compounds are protected from degradation when stabilized by interaction with mineral crystal aggregates (
31). In addition, by adsorbing to a stabilizing mineral matrix, biomolecules are effectively isolated from water, thereby retarding hydrolytic damage (
32)."
See? Proteins break down in high oxygen conditions. But oxygen is lacking in the canals in bones of very large animals. Then they are further protected by interacting with the mineral crystals. Far from indicating a young age for the dinos, they indicate nothing more than normal chemistry.
Now, let's look at this particular specimen:
" A near-complete specimen of the Late Cretaceous dinosaur
Tyrannosaurus rex [Museum of Rockies (MOR) 555] was collected by MOR from the Hell Creek formation (6765 million years ago) of eastern Montana in 1990. The completeness and articulation of the skeleton indicated that burial was rapid enough to forestall damage by scavenging and weathering but not rapid enough to prevent some minimal displacement. The specimen was surrounded by a consolidated white sandstone, buried under 11.5 m of stream channel sediments that contained abundant coalified plant material. The specimen was collected with 0.50.6 m of sediment in place between the unexposed hind limb used in this study and the pelvis, which had been exposed before collection. Preliminary examination of trabecular bone elements of the specimen revealed little or no evidence of internal permineralization or replacement. This relatively unaltered state may be due to minimal exposure to water. Dehydration would favor preservation of endogenous biomolecules, including hemoglobin, so an attempt was made to detect their presence in the tissues of MOR 555."
Special conditions of preservation here.
Even so, looking at the Abstract, we can see that the preservation was not enough to give sufficient quantities for an amino acid analysis. Most hemoglobin in the bone was indeed completely degraded. The presence was
inferred through indirect means, not direct observation. BTW, these are the types of observations -- indirect -- that creationists say are not valid in other contexts. The irony is apparent.
Now, is the hemoglobin
intact?
NO!
"The proton NMR spectrum of the dinosaur extracts (Fig.
2) contains peaks upfield and downfield from the standard 0- to 10-ppm window characteristic of the resonances of protons in proteins and other organic molecules. Four broad resonances at 25.0, 29.0, 45.0, and 72.0 ppm, as well as three other peaks at −9.0, −20.0, and −30.0 ppm indicate the presence of a paramagnetic atom, such as those seen in various metalloproteins (
44,
45).
The spectrum is consistent with degraded heme proteins in the met (Fe3+) state (
6,
45).
Notice that word "degraded".
"Significant levels of
D-enantiomers of individual amino acids (39) suggest that the source proteins are ancient."
What isomer are amino acids in living animals?
L-amino acids. Not D. What we have here is amino acids that have been racemized over a long period of time. Longer than 6,000 years.
"
"
None of the analytical results obtained was completely identical to those noted experimentally or in the literature for modern hemoglobins. However, ancient molecules typically show variations in analytical profiles from their purified modern counterparts because of chemical modifications during degradation (
49,
25). Geochemical interactions with biomolecules preserved in fossil bone over millions of years are to be expected, and the presence of additional, nonhemoglobin signals detected by the various physical methods is not unexpected given the highly degraded and diagenetically altered biological compounds in the bone."
Any claim that "hemoglobin" was isolated is false witness. What we have are the
degredation products of hemoglobin, not the molecule itself.
