Reinigung und Eigenschaften der Glutamin-Synthetase aus Schweinehirn

Abstract

Glutamine synthetase from pig brain was enriched more than 200 fold, and crystallized. The particle weight is 415,000; the enzyme consists of at least 8 subunits. The enzyme constants and the effect of different inhibitors on the enzymatic reaction were determined. The Michaelis constant for L-glutamic acid was dependent on the pB; it is concluded that a histidine residue is involved in the binding of L-glutamate. SH-groups are involved in the binding of ATP [adenosine triphosphate]. Four molecules of glutamtc acid are bound per molecule of enzyme.