Open AccessCrystalline 6‐Phosphogluconate Dehydrogenase from Sheep Liver
Author(s) -
Silverberg Michael,
Dalziel Keith
Publication year - 1973
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1973.tb03054.x
Subject(s) - dehydrogenase , enzyme , chemistry , biochemistry , protein subunit , gene
6‐Phosphogluconate dehydrogenase has been obtained in the pure, crystalline form from sheep liver by an extensive modification of an earlier purification procedure. The absorption coefficient, A 1% 280 , estimated from dry weight measurements, is 11.4. The amino acid composition is reported. The molecular weight of the enzyme from measurement by several methods is 94000 ± 2000, and there are two subunits in the molecule. From studies of the reaction of the native enzyme with 5,5′‐dithiobis(2‐nitrobenzoic acid) and p ‐hydroxymercuribenzoate, there appear to be two reactive thiol groups per subunit which are essential for activity and are protected by 6‐phosphogluconate or NADPH.