Peptide Bond Cleavage on Trypsintrypsin Inhibitor Complex Formation.
نویسندگان
چکیده
منابع مشابه
The Basic Trypsin Inhibitor of Bovine Pancreas IX. LOCATION OF THE REACTIVE SITE IN THE CARBOXAMIDOMETHYL
A derivative of the basic pancreatic inhibitor which contained carboxamidomethyl groups on half-cystine residues 14 and 38 was incubated with trypsin and intact inhibitor at pH 5.5. The carboxamidomethyl derivative after separation from trypsin and intact inhibitor released only lysine when incubated with carboxypeptidase B. The derivative was oxidized with performic acid and a peptide correspo...
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A derivative of the basic pancreatic inhibitor which contained carboxamidomethyl groups on half-cystine residues 14 and 38 was incubated with trypsin and intact inhibitor at pH 5.5. The carboxamidomethyl derivative after separation from trypsin and intact inhibitor released only lysine when incubated with carboxypeptidase B. The derivative was oxidized with performic acid and a peptide correspo...
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Human C1-inhibitor (C1-Inh) forms an equimolar complex with complement proteinase C1s that is resistant to dissociation by sodium dodecyl sulfate. The formation of this stable complex results in the cleavage of a peptide bond near the carboxyl terminus of the inhibitor and, whereas the bulk of C1-Inh remains covalently bound to the light chain of C1s, the postcomplex inhibitor peptide can be is...
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عنوان ژورنال:
- The Journal of biological chemistry
دوره 240 شماره
صفحات -
تاریخ انتشار 1965