虹鳟（Salmo gairdneri）脑中金属硫蛋白的纯化、特性鉴定及其对磷酸吡哆醛激酶的激活作用

Purification and characterization of metallothionein and its activation of pyridoxal phosphokinase in trout (Salmo gairdneri) brain.

Hao R, Pfeiffer R F, Ebadi M

Section of Neurology, University of Nebraska College of Medicine, Omaha 68198-6260.

Comp Biochem Physiol B. 1993 Feb;104(2):293-8. doi: 10.1016/0305-0491(93)90371-b.

Abstract

Brain metallothionein was isolated and purified for the first time from rainbow trout. 2. Brain metallothionein exhibited an elution volume (Ve/Vo) of 2.0, had a molecular weight of 6762 Daltons, and contained a zinc content of 9 micrograms/mg protein. 3. Brain pyridoxal phosphokinase was isolated and assayed for the first time in rainbow trout. 4. Zinc (0.20 microM) or zinc metallothionein (6-30 microM) stimulated the activity of brain pyridoxal kinase in a linear fashion. 5. The results of these studies are interpreted to suggest that in trout brain zinc metallothionein may participate in metabolism of vitamin B6 and formation of pyridoxal phosphate, the active coenzyme.

摘要

首次从虹鳟鱼中分离并纯化出脑金属硫蛋白。2. 脑金属硫蛋白的洗脱体积（Ve/Vo）为2.0，分子量为6762道尔顿，蛋白质中锌含量为9微克/毫克。3. 首次在虹鳟鱼中分离并测定了脑吡哆醛磷酸激酶。4. 锌（0.20微摩尔）或锌金属硫蛋白（6 - 30微摩尔）以线性方式刺激脑吡哆醛激酶的活性。5. 这些研究结果表明，在鳟鱼脑中，锌金属硫蛋白可能参与维生素B6的代谢和活性辅酶磷酸吡哆醛的形成。