Purification and Characterisation of Adenosine‐3′,5′‐Phosphate‐Independent Protein Kinase from Wheat Germ

Abstract

CAMP-independent protein kinase was isolated from the wheat germ and purified to electrophoretic homogeneity. The molecular weight of enzyme was approximately 20000, K_m for ATP was (1 ± 0.2) × 10⁻⁵ M. V was 215 nmol phosphate mg enzyme⁻¹ min⁻¹, and the isoelectric point was at pH 9.2. The enzyme promotes phosphorylation of casein and crude wheat germ ribosomes.