Specificity of ProteolysisSpecificity of Proteolysis presents a survey and conclusions on the action or proteinases - enzymes which are cleaving proteins or peptides. The specificity of proteinases which is determined as the sequence of amino acids at the cleavage site of a substrate, is an important criteria to choose an enzyme as tool in protein research. Whenever one is looking for an enzyme to act at a defined site or to give defined cleavage products one will find comprehensive information in this work. Comprehensive information about more than 280 endopeptidases which are based on the database LYSIS including a calculation program to determine cleavage sites, is given in the book. |
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Acad Acta activity Agkistrodon alpha amino acid residues angiotensin asp-p aspartic endopeptidase Aspergillus B-chain of insulin Bacillus beta Biochem Biochemistry Biol Biophys Bos taurus Bovine Cathepsin cathepsin D cells chain Chem chymotrypsin cleavage cleavages produced cleaves bonds cleaves preferentially bonds Coagulation factor collagen collagenase Crotalus degrades EDTA elastase endopeptidase Source enzyme enzyme cleaves enzyme was isolated erythrocyte Escherichia coli extracellular FEBS Lett Gallus gallus glucagon Homo sapiens Homo sapiens plasma Hoppe-Seyler's Human hydrophobic hydrophobic residues Immunoglobulin inhibited by DFP inhibited by EDTA inhibitors EC inhibitors The enzyme insulin kallikrein Keil ketone membrane metalloendopeptidase metalloproteinase Methods Enzymol Morihara neutral endopeptidase o-phenantroline ovomucoid pancreatic pepsin Physiol pituitary PMSF polypeptidic substrates porcine position P₁ Proc protease Pseudomonas Rattus norvegicus residues in position Review Ribosomal protein scrofa sequence serine endopeptidase serine proteinase soybean trypsin inhibitor Specificity The enzyme Streptomyces Subtilisin synthetic peptides synthetic substrates venom Wittmann-Liebold