RAPID METHOD FOR THE PURIFICATION OF OCTOPINE DEHYDROGENASE FOR THE DETERMINATION OF CELL METABOLITES

被引：12

作者：

GADE, G ^{[1
]}

HEAD, EJH ^{[1
]}

机构：

[1] NERC,MARINE SCI LABS,MARINE INVERTEBRATE BIOL UNIT,MENAI BRIDGE,GWYNEDD,WALES

来源：

EXPERIENTIA | 1979年 / 35卷 / 03期

关键词：

D O I：

10.1007/BF01964314

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

Unlike other NAD+-dependent dehydrogenases, octopine dehydrogenase was not bound by blue Sepharose. A rapid 2-step purification procedure (gel filtration on Sephadex G-100 followed by affinity chromatography on blue Sepharose) resulted in a final preparation of octopine dehydrogenase which had a sp. act. of 65 units/mg protein and was free of contaminating NAD+-oxidoreductases. This preparation has been used successfully for the estimation of phospho-L-arginine, L-arginine and octopine in perchloric acid extracts. © 1978 Birkhäuser Verlag.

引用

页码：304 / 305

页数：2

共 13 条

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