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- W2091739969 abstract "Abstract Insulin, which contains two internally situated asparagine residues and one C-terminal asparagine residue, was used as a model compound to study the specificity of protein hydrolysis in dilute hydrochloric acid. Changes occurring in aspartic acid, ammonia (arising from the hydrolysis of amide bonds), and α-amino nitrogen were determined throughout the course of hydrolysis. The results indicated that quantitative cleavage of asparagine and glutamine amide bonds and aspartic acid peptide bonds occurred. Determinations of N-terminal residues in insulin partial hydrolyzates revealed that cleavage of some serine and threonine peptide bonds occurred, but no other unexpected N-terminal residues were noted. The fragmentation in dilute acid of the proteins of the albumin fraction of human serum was studied by measuring changes in the total α-amino nitrogen content of four subfractions of albumin partial hydrolyzates, and additional evidence concerning the specificity of dilute acid hydrolysis was obtained. A peptide was isolated in good yield from an albumin dilute acid hydrolyzate and was partially characterized." @default.
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- W2091739969 date "1960-12-01" @default.
- W2091739969 modified "2023-10-17" @default.
- W2091739969 title "The hydrolysis of insulin and human serum albumin in dilute hydrochloric acid" @default.
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- W2091739969 doi "https://doi.org/10.1016/0003-9861(60)90499-9" @default.
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