| Literature DB >> 14212151 |
Abstract
Lambda coli phage is not inactivated by chymotrypsin, trypsin, or ficin. T(2) phage is slowly inactivated by high concentrations of (alpha-, beta-, gamma-, or Delta-chymotrypsin, but not by trypsin or ficin. P(1) phage is slowly inactivated by alpha-, beta-, or gamma-chymotrypsin, or ficin, more rapidly by Delta-chymotrypsin, and much more rapidly by trypsin. Crystalline egg albumin, crystalline serum albumin, E. coli nucleoprotein, and yeast nucleoprotein are hydrolyzed slowly by alpha-chymotrypsin. Yeast nucleoprotein, like P(1) phage, is hydrolyzed more rapidly by Delta-chymotrypsin than by alpha-chymotrypsin, but not by trypsin or ficin. Neither phages nor native proteins were attacked by papain, carboxypeptidase, deoxyribonuclease, or ribonuclease.Entities:
Keywords: CARBOXYPEPTIDASES; CHYMOTRYPSIN; COLIPHAGES; DEOXYRIBONUCLEASE; EXPERIMENTAL LAB STUDY; KINETICS; NUCLEOPROTEINS; OVALBUMIN; PAPAIN; PEPTIDE PEPTIDOHYDROLASES; RIBONUCLEASE; SERUM ALBUMIN; TRYPSIN; YEASTS
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Year: 1964 PMID: 14212151 PMCID: PMC2195401 DOI: 10.1085/jgp.48.1.73
Source DB: PubMed Journal: J Gen Physiol ISSN: 0022-1295 Impact factor: 4.086