[Purification, molecular weight and subunit structure of NAD(NADP)-dependent glyceraldehyde 3-phosphate dehydrogenase from Chlorella].

The NAD(NADP) dependent glyceraldehyde 3-phosphate dehydrogenase was isolated from the thermophylic strain of Chlorella pyrenoidosa Pringsheim 82T. The isolation and purification procedures included fractionation of the proteins with (NH4)2SO4, column chromatography on Bio-Gel A-1,5 m and rechromatography on hydroxyapatite. The enzyme was homogeneous during electrophoresis in polyacrylamide gel. The molecular weight of the oligomeric enzyme is 160 000, that of the subunits is 40 000. The amino acid composition and total number of SH-groups were determined.