PURIFICATION AND CHARACTERIZATION OF 2 FORMS OF SOLUBLE NADH CYTOCHROME-B5 REDUCTASES FROM HUMAN ERYTHROCYTES
COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY B-BIOCHEMISTRY & MOLECULAR BIOLOGY, vol.101, pp.235-242, 1992 (SCI-Expanded, Scopus)
- Publication Type: Article / Article
- Volume: 101
- Publication Date: 1992
- Doi Number: 10.1016/0305-0491(92)90185-t
- Journal Name: COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY B-BIOCHEMISTRY & MOLECULAR BIOLOGY
- Journal Indexes: Science Citation Index Expanded (SCI-EXPANDED), Scopus
- Page Numbers: pp.235-242
- Middle East Technical University Affiliated: Yes
Abstract
1. Two forms of soluble NADH cytochrome b5 reductase were purified from human erythrocytes. Two distinct fractions both having the NADH cytochrome b5 reductase activity eluted from the second DEAE-cellulose column were further purified by ultrafiltration and 5'-ADP-agarose affinity chromatography.