Cleavage of the two methionine residues in the glycoprotein trypsin inhibitor ovomucoid, variant 01, with CNBr resulted in two fragments whose mol.wts. were approx. 16 600 (fragment LS) and 11000 (fragment M). Both fragments formed precipitates with antisera to ovomucoid. Fragment LS retained 56 % of the trypsin-inhibitory activity of ovomucoid, but fragment M did not inhibit. After reduction and alkylation, the molecular weight of fragment M was unchanged, but fragment LS could be resolved into two segments of peptide chain with mol
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