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  • [Kinetics of L-gamma-Glu-pNA hydrolysis by destabilase, the enzyme from the medicinal leech Hirudo medicinalis].

[Kinetics of L-gamma-Glu-pNA hydrolysis by destabilase, the enzyme from the medicinal leech Hirudo medicinalis].

Biokhimiia (Moscow, Russia) (1990-04-01)
I P Baskova, G I Nikonov, L L Zavalova, N I Larionova
ABSTRACT

The molecular mass of destabilase isolated from the medicinae leech Hirudo medicinalis was found to be equal to 12.3 kDa. A kinetic analysis of the sole presently known synthetic substrate, L-gamma-Glu-pNA, showed that the enzyme is relatively stable to heating (5 min, 70 degrees C); the pH optimum lies at 7.0-8.5. The enzyme has a specific activity of 0.15 x 10(-9) mol.s-1.mg-1; Km = 2.2 x 10(-4) M, kcat is 3.53 x 10(-3) s-1 (pH 8.0, 37 degrees C).

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
L-Glutamic acid γ-(4-nitroanilide), γ-glutamyl transpeptidase substrate
Sigma-Aldrich
L-Glutamic acid γ-(p-nitroanilide) hydrochloride, γ-glutamyl transpeptidase substrate