Abstract
DURING an investigation of the early stages of hydrolysis of various mucoids and connective-tissue proteins, it was observed that, on partial hydrolysis with acetic acid or oxalic acid at 100°, aspartic acid was in each case the first amino-acid to appear in the free condition, followed at a somewhat later stage by glutamic acid1. Since elastin has an unusually low content of the dicarboxylic amino-acids2, it was thought that, with this protein, hydrolytic cleavage at some proportion of the aspartic or glutamic acid residues might yield soluble degradation products of high molecular weight.
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References
Partridge, S. M., and Davis, H. F., Nature, 165, 62 (1950).
Neuman, R. E., Arch. Biochem., 24, 289 (1949).
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ADAIR, G., DAVIS, H. & PARTRIDGE, S. A Soluble Protein derived from Elastin. Nature 167, 605 (1951). https://doi.org/10.1038/167605a0
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DOI: https://doi.org/10.1038/167605a0
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