Cleavage Specificity of Boar Acrosin on Polypeptide Substrates, Ribonuclease and Insulin B-Chain
| Autor: | Hans Fritz, Wolf-Dieter Schleuning, Schiessler H |
|---|---|
| Rok vydání: | 1975 |
| Předmět: |
Male
BOAR Swine medicine.medical_treatment macromolecular substances Benzoylarginine Nitroanilide Arginine Cleavage (embryo) Biochemistry Hydrolysis Ribonucleases Endopeptidases medicine Animals Insulin Peptide bond Trypsin Ribonuclease Acrosin Binding Sites biology Chemistry Lysine Peptide Fragments Kinetics biology.protein Cattle medicine.drug |
| Zdroj: | Hoppe-Seyler´s Zeitschrift für physiologische Chemie. 356:1931-1936 |
| ISSN: | 0018-4888 |
| Popis: | The cleavage specificity of boar acrosin is, like that of trypsin, strictly limited to the arginyl and lysyl bonds, as demonstrated for the oxidized B-chain of insulin. In addition, in this polypeptide substrate as well as in reduced and carboxymethylated ribonuclease, these peptide bonds are hydrolyzed by acrosin and trypsin with nearly identical velocities. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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