[Acid proteinase from the roe of the trout Salmo gairdneri R].
Acidic proteinase from the trout spawn is 640 fold purified (yield 22%). Purification includes autolysis, acid treatment, ammonium sulphate fractionation, G-100 Sephadex gel-filtration, ion-exchange chromatography on DEAE-cellulose. Molecular mass of the enzyme under study is 70 kDa according to the data of gel-filtration. Acidic proteinase displays its greatest activity towards hemoglobin (pH 4.0, 37 degrees C) and is inhibited completely by EDTA, by 50%--by Pb2+ and soya inhibitor of trypsin and 2.8 times activated by Zn2+. Enzyme activity is not affected by dithiotreitol, iodine acetate, phenylmethylsulphonylfluoride parachloromercurybenzoate, Hg2+, Na+, Co2+, Ca2+.
D000818:Animals; D016282:Aspartic Acid Endopeptidases; D001665:Binding Sites; D002848:Chromatography, DEAE-Cellulose; D002850:Chromatography, Gel; D010450:Endopeptidases / Q000302:isolation & purification* / Q000378:metabolism; D005260:Female; D006863:Hydrogen-Ion Concentration; D008970:Molecular Weight; D010063:Ovum / Q000032:analysis*; D012487:Salmonidae / Q000378:metabolism*; D014337:Trout / Q000378:metabolism*
D010450:Endopeptidases; D016282:Aspartic Acid Endopeptidases
Kislaia proteinaza iz ikry raduzhnoĭ foreli Salmo gairdneri R.