COMPARATIVE STUDIES OF GALACTOKINASE ACTIVITY ON MAMMALS RED BLOOD-CELLS

被引：7

作者：

MAGNANI, M

CUCCHIARINI, L

STOCCHI, V

BOSSU, M

DACHA, M

FORNAINI, G

机构：

[1] Istituto di Chimica Biologica, Universitá degli Studi di Urbino, Urbino, Via Saffi

来源：

COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY B-BIOCHEMISTRY & MOLECULAR BIOLOGY | 1979年 / 64卷 / 03期

关键词：

D O I：

10.1016/0305-0491(79)90141-X

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：

1. 1. ATP: d-galactose-1-phosphotransferase activity was measured in human, pig, cow, rabbit, mouse and rat red blood cells. Mean values of galactokinase activity was markedly lower in the human and pig erythrocyte as compared to those of the other species. 2. 2. The permeability to galactose of the red cells studied was always higher than galactose phosphorylation. 3. 3. The affinity constants of galactokinase for galactose ranged from 119 to 291 μM and from 178 to 406 μM for ATPMg2-. 4. 4. The thermostability values of the galactokinase of the species studied were similar. The pH-optimum is pH 7.5 for the human, mouse and rabbit enzyme and pH 8.0 for cow, pig and rat galactokinase. © 1979.

引用

页码：267 / 271

页数：5

共 22 条

[1] PURIFICATION AND PROPERTIES OF GALACTOKINASE FROM PIG LIVER [J].