SH-proteinase from bean Phaseolus vulgaris var. Perlicka.
An SH-proteinase (EC 3.4.22.-) has been isolated from beans of the species Phaseolus vulgaris var. Perlicka. The enzyme is homogeneous when subjected to disc electrophoresis, electrofocusing and sedimentation analysis. The molecular weight was determined as 26,000-28,000 by gel filtration, 30,850 +/- 1500 by sedimentation analysis and 26,930-27,410 by calculation from the amino acid composition (Lys20-21, His3, Arg9, Asp21-22, Thr13, Ser18, Pro12-13, Glu23-24, Gly30, Ala16, Cys/29, Val19, Met1, Ile10, Leu13, Tyr14, Phe6, Trp3). The N-terminal amino acid of the proteinase is isoleucine. The effect of concentration, time of hydrolysis, pH, temperature, cations, anions, urea and guanidine - HCl on the proteolytic activity of the SH-proteinase was studied.
D000596:Amino Acids / Q000032:analysis; D004355:Drug Stability; D006146:Guanidines / Q000494:pharmacology; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008970:Molecular Weight; D010447:Peptide Hydrolases / Q000032:analysis* / Q000302:isolation & purification / Q000378:metabolism; D010944:Plants / Q000201:enzymology*; D011485:Protein Binding; D013438:Sulfhydryl Compounds / Q000032:analysis; D013696:Temperature; D014508:Urea / Q000494:pharmacology
D000596:Amino Acids; D006146:Guanidines; D013438:Sulfhydryl Compounds; D014508:Urea; D010447:Peptide Hydrolases