Inactivation of α-Chymotrypsin by a Water-soluble Carbodiimide
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چکیده
منابع مشابه
Inactivation of chymotrypsin by diphenyldiazomethane.
a-Chymotrypsin is a protein composed of three peptide chains linked by disulfide bridges, with amino-terminal half-cystine, isoleucine, and alanine residues.1 The latter two end groups appear upon the enzymic conversion of chymotrypsinogen A (which only contains the amino-terminal half-cystine residue) to a-chymotrypsin. The specificity of a-chymotrypsin as an enzyme (and of other chymotrypsins...
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In TTX-sensitive nerve and skeletal muscle Na+ channels, selective modification of external carboxyl groups with trimethyloxonium (TMO) or water-soluble carbodiimide (WSC) prevents voltage-dependent Ca2+ block, reduces unitary conductance, and decreases guanidinium toxin affinity. In the case of TMO, it has been suggested that all three effects result from modification of a single carboxyl grou...
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A cross-linking method for collagen-based biomaterials was developed using the water-soluble carbodiimide 1-ethyl-3-(3-dimethyl aminopropyl)carbodiimide hydrochloride (EDC). Cross-linking using EDC involves the activation of carboxylic acid groups to give O-acylisourea groups, which form cross-links after reaction with free amine groups. Treatment of dermal sheep collagen (DSC) with EDC (E-DSC)...
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Bacterial collagenase was used to study the susceptibility of dermal sheep collagen (DSC) cross-linked with a mixture of the water-soluble carbodiimide 1-ethyl-3-(3-dimethyl aminopropyl)-carbodiimide hydrochloride and N-hydroxysuccinimide (E/N-DSC) towards enzymatic degradation. Contrary to non-cross-linked DSC (N-DSC), which had a rate of weight-loss of 18.1% per hour upon degradation, no weig...
متن کاملPartial and selective inactivation of thrombokinase by chymotrypsin.
Thrombokinase has been isolated from bovine plasma in a form that approached electrophoretic homogeneity` and gave a single boundary in the ultracentrifuge.' Such material has four separately measurable activities: 1. activation of prothrombin in the presence of oxalate; 2. activation of prothrombin in the presence of ionic calcium, phospholipid and factor V; 3. activation of chymotrypsinogen; ...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1969
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)63469-6