PURIFICATION AND DETERMINATION OF THE BINDING-SITE OF LACTATE-DEHYDROGENASE FROM CHICKEN BREAST MUSCLE ON IMMOBILIZED FERRIC IONS

被引：19

作者：

CHAGA, G

ANDERSSON, L

PORATH, J

机构：

[1] UNIV UPPSALA,CTR BIOCHEM SEPARAT,BOX 577,S-75123 UPPSALA,SWEDEN

[2] INST BIOPROD,BU-4003 PLOVDIV,BULGARIA

来源：

JOURNAL OF CHROMATOGRAPHY | 1992年 / 627卷 / 1-2期

关键词：

D O I：

10.1016/0021-9673(92)87196-F

中图分类号：

O65 [分析化学];

学科分类号：

070302 ; 081704 ;

摘要：

Lactate dehydrogenase from chicken breast muscle was purified to homogeneity in one step by immobilized metal ion affinity chromatography. The purified enzyme was used to localize the binding site to immobilized Fe(III) ions. After cyanogen bromide degradation and digestion with trypsin, small enzyme fragments capable of binding to immobilized Fe(III) ions were obtained. It is proposed that several histidyl groups are involved in the binding.

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页码：163 / 172

页数：10

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