Properties and specificity of the major anionic trypsin-like enzyme in the keratinolytic larvae of the webbing clothes moth.
Biochim Biophys Acta, 1975/5/23;391(1):201-11.
PMID: 237556
Abstract
The major form of the trypsin-like proteinases from the larvae of the webbing clothes moth Tineola bisselliella has been further purified and some of its properties investigated. It differs from bovine trypsin in several respects. It is anionic at neutral pH, is very stable at alkaline pH, has no requirement for calcium ions for this stability and is very sensitive to urea. It resembles vertebrate trypsins in its complete inhibition by diisopropylfluorophosphate, its pH optimum of 8.5 for hydrolysis of benzoyl-arginine p-nitroanilide and its cleavage specificity against glucagon and the beta-chain of S-carboxymethyl insulin.
MeSH terms
Amino Acids; Animals; Binding Sites; Calcium; Cattle; Drug Stability; Glucagon; Hydrogen-Ion Concentration; Insulin; Isoflurophate; Keratins; Kinetics; Larva; Lepidoptera; Mathematics; Moths; Peptide Fragments; Protein Binding; Protein Conformation; Species Specificity; Trypsin; Urea
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