The determination of hydroxyproline in tissue and protein samples containing small proportions of this imino acid.
01 May 1961-Archives of Biochemistry and Biophysics (Arch Biochem Biophys)-Vol. 93, Iss: 2, pp 440-447
TL;DR: Method has been applied to a study of hydroxyproline distribution in cell particulates, tissue fluids, and purified plant and animal proteins, and significant amounts of hydroXYproline were found in crystalline preparations of pepsin, elastase.
About: This article is published in Archives of Biochemistry and Biophysics.The article was published on 1961-05-01. It has received 3756 citations till now. The article focuses on the topics: Hydroxyproline & Imino acid.
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Cites methods from "The determination of hydroxyproline..."
...Collagen level was determined by analyzing the hydroxyproline content in newly regenerated tissue [67]....
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TL;DR: A short and simple calorimetric method is here described that is applicable to the determination of hydroxyproline in hydrolysates of 40 to 100 y of collagen with a reproducibility of f2 per cent and an accuracy of f1 per cent as judged by recovery of hydroXYproline from elastin hydrolysate and from an amino acid mixture simulating collagen.
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TL;DR: Stetten (1949) suggested that free hydroxyproline was not an intermediate in collagen biosynthesis and that hydroxylation of the proline residues occurred at the protein or peptide stage.
Abstract: Stetten & Schoenheimer (1943) fed [15N]proline to young rats and showed it to be a good source of the hydroxyproline of the carcass protein. Later, Stetten (1949) found that the efficiency of dietary [15N]hydroxyproline was less than one-twentieth of that of proline as a precursor of collagen hydroxyproline. These findings are of considerable interest since they are contrary to the general observation that proteins are built up from their constituent free amino acids (Loftfield, 1957). The only close parallel, discovered subsequently, is the formation of collagen hydroxylysine from lysine (Sinex & Van Slyke, 1955; Piez & Likins, 1957), but not from free hydroxylysine (Sinex & Van Slyke, 1957). Stetten (1949) suggested that free hydroxyproline was not an intermediate in collagen biosynthesis and that hydroxylation of the proline residues occurred at the protein or peptide stage. The hydroxylation of
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