The fidelity of albumin biosynthesis in aged C57B1 mice
Date Issued
December 1, 1981
Author(s)
Burke, James R.
Advisor(s)
M. P. Stulberg
Additional Advisor(s)
Francis T. Kenney
Abstract
The fidelity of albumin biosynthesis in 3- and 30-month-old C57B1 male mice was assessed. Albumin was isolated from serum and liver by immunoaffinity chromatography and monitored by double immunodiffusion throughout isolation. Two-dimensional gel electrophoresis was used to detect possible alterations in the isoelectric point and size of albumin from serum and liver as a function of age. No differential heterogeneity in albumin was found, thus no amino acid substitutions involving charge changes or modification of molecular weight occurred with aging of the animals. The hydrophobic properties of fragmented and alkylated albumin were examined by Triton X-100 polyacrylamide gel electrophoresis and found to be unaltered with age, thus neutral amino acid substitutions had not occurred. The molecular conformation and net charge of albumin, assayed by gel sieving electrophoresis at acidic and basic pH, were identical in the 3- and 30-month-old mice. In contrast to the albumin data, a striking quantitative difference between the serum of young and old animals was observed in what was tentatively identified as transferrin.
Degree
Doctor of Philosophy
Major
Biomedical Sciences
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Thesis81b.B872.pdf
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