Abstract
Summary
The mechanism of albumin biosynthesis in rabbit liver was investigated in vivo by observing the pattern of lysine incorporation in albumin isolated from a rabbit injected with DL-1-C14 lysine via a mesenteric vein. Peptides were obtained by chromatographing tryptic hydrolysates of the albumin. Radioactivity measurements were made on lysine chromatographically isolated from individual acid-hydrolyzed peptides and quantitative lysine determinations were made with the automatic amino acid analyzer. The results indicated nonuniform labeling of the lysine residues in serum albumin which persisted for as long as 4 hours after isotope injection. It is postulated that the unequal labeling and its long duration were demonstrable because of the “pulse” nature of the introduction of the isotope to the synthesizing system.
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