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• W2033137078 abstract "The two methionyl peptide bonds of lysozyme of human origin were cleaved by cyanogen bromide in 70 per cent formic acid. Cleavage was shown by the absence of methionine and the appearance of homoserine and homoserine lactone on amino acid analysis, detection of two new amino groups, and separation of the expected peptides upon Sephadex gel filtration. The products were shown to consist of a free single polypeptide chain (residues 18–29) and a remaining molecule with two polypeptide chains (residues 1–17 and 30–129) held together by 4 disulfide bridges. The enzymatic activity of the cyanogen bromide treated lysozyme or of its products was destroyed. Immunological studies revealed that both CNBr products can react with antibodies prepared against native lysozyme. This was demonstrated by their ability to; (a) inhibit the inactivation of human lysozyme-T4 bacteriophage conjugate; (b) to bind specifically to antibody-Sepharose conjugate and (c) to cause inhibition of the binding of radioactively labelled human lysozyme by anti-human lysozyme serum." @default.
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• W2033137078 date "1971-09-01" @default.
• W2033137078 modified "2023-09-27" @default.
• W2033137078 title "Structural basis for immune recognition of lysozymes-IV. Immunologically active peptide obtained by the action of cyanogen bromide on human lysozyme" @default.
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• W2033137078 doi "https://doi.org/10.1016/0019-2791(71)90449-6" @default.
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