Biomedical subjects
Publications and source records attributed to F D Davidson.
1. A study has been made of the gelatins obtained by treating a number of fresh and fossil collagens with dilute formic acid. 2. Compositions of their peptides separated by filtration through polyacrylamide gels has been established. 3. Solubilization results in the freeing of much aspartic acid and less glycine, the amounts being determined for the collagens investigated.
1. Studies have been made of products obtained by treating several reptilian fossil bones with dilute formic acid. 2. Their amounts and compositions have been compared with those of similarly treated fresh and Pleistocene bones. 3. Fewer and small peptides are obtained from the older fossils but in only one instance was the composition significantly different from that of the total protein. 4. For the collagenous proteins aspartic acid was the most readily freed by hydrolysis; for these older proteins it is alanine. 5. Unlike the Pleistocene proteins, the chromatograms from these older proteins have always had peaks in the position of beta-alanine, and usually others of unidentified origin.
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More than 90% of the protein in the shells of the modern oyster, Ostrea angelica, is decomposed when shells are heated at 130 degrees for 1 week. There remains, however, a stable residue that is little changed as heating is continued for 9 weeks. This residue resembles, in both amount and composition, the material previously recovered from fossil oyster shells deposited before the Pliocene era.
Analyses of the protein residues recovered from fossil oyster shells of ages from the Pleistocene through the Cretaceous show substantially the same amino acids as are present in modern proteins. The amount of these residues declines sharply to the Oligocene, after which it proceeds more slowly. These older proteins contain relatively less aspartic acid and glycine than do their younger counterparts.