1. Properties of the Antheraea mylitta cocoonase
- Author
-
R.L. Felsted, John H. Law, M. S. Jolly, and Amit Sinha
- Subjects
Chromatography, Gas ,Arginine ,Physiology ,Cocoonase ,Proteolysis ,Carbohydrates ,Biology ,Tritium ,Biochemistry ,chemistry.chemical_compound ,Antheraea mylitta ,Endopeptidases ,medicine ,Centrifugation, Density Gradient ,Animals ,Trypsin ,Amino Acid Sequence ,Amino Acids ,Molecular Biology ,Peptide sequence ,chemistry.chemical_classification ,Autoanalysis ,Binding Sites ,medicine.diagnostic_test ,Proteolytic enzymes ,Metamorphosis, Biological ,Sodium Dodecyl Sulfate ,General Medicine ,Bombyx ,Molecular biology ,Chymotrypsinogen ,Enzyme Activation ,Molecular Weight ,Kinetics ,Enzyme ,chemistry ,Chromatography, Gel ,Electrophoresis, Polyacrylamide Gel ,Spectrophotometry, Ultraviolet ,Chromatography, Thin Layer ,Lysozyme ,Peptides ,Peptide Hydrolases - Abstract
1. 1. The proteolytic enzyme, cocoonase, from Antheraea mylitta has been compared to other cocoonases and bovine trypsin and found to be similar in (1) molecular weight, (2) amino acid composition, (3) specificity and reactivity toward Nα-benzoyl- l -arginine ethyl ester, (4) proteolytic specificities toward glucagon, B-chain of insulin and lysozome, (5) rate of proteolysis of modified lysozyme and (6) NH2-terminal amino acid sequence. 2. 2. The A. mylitta cocoonase, however, activated chymotrypsinogen A at a rate 3200-fold slower than bovine trypsin which suggested subtle and important differences in the structures of these two enzymes.
- Published
- 1973