HIGH-MOLECULAR-WEIGHT HEAT-STABLE ALKALINE PROTEINASE FROM WHITE CROAKER AND CHUM SALMON MUSCLE - COMPARISON OF THE ACTIVATING EFFECTS BY HEATING AND UREA

被引：16

作者：

TOYOHARA, H

NOMATA, H

MAKINODAN, Y

SHIMIZU, Y

机构：

[1] KYOTO UNIV, FAC AGR, DEPT FISHERIES, SAKYO KU, KYOTO 606, JAPAN

[2] HOKKAIDO KUSHIRO FISHERIES EXPTL STN, KUSHIRO 085, JAPAN

[3] KINKI UNIV, FAC AGR, DEPT FISHERIES, HIGASHIOSAKA, OSAKA 577, JAPAN

来源：

COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY B-BIOCHEMISTRY & MOLECULAR BIOLOGY | 1987年 / 86卷 / 01期

关键词：

D O I：

10.1016/0305-0491(87)90181-7

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Effects of heating and urea on the heat-stable alkaline proteinase from white croaker and chum salmon muscle were compared in order to know the regulating mechanism of the proteinase. Chum salmon proteinase required a higher temperature for activity and was more heat-stable than white croaker proteinase. In the presence of 5M urea, the activity was observed to some degree at 37.degree.C only in white croaker proteinase, while both proteinases lost their activities at usual assay temperature around 60.degree.C. These results suggest that the stability of the regulatory and catalytic subunits of the proteinases is somewhat different among fish species.

引用

页码：99 / 102

页数：4

共 14 条

[1] IDENTIFICATION OF 2 ALKALINE PROTEASES AND A TRYPSIN-INHIBITOR FROM MUSCLE OF WHITE CROAKER (MICROPOGON-OPERCULARIS) [J].