Oct 1, 1975

Highly purified glutamine transaminase from rat brain. Physical and kinetic properties

European Journal of Biochemistry
F Van Leuven


Glutamine transaminase from rat brain was purified to a high degree. The isolated enzyme appeared to be homogeneous by electrophoresis on polyacrylamide gel. The molecular weight was found to be approximately 98 000; the enzyme is probably composed of two subunits. The absorbance maximum at 410 nm and the inhibition by carbonyl reagents are strong indications for the presence of pyridoxal phosphate. The enzyme showed maximal activity at pH 9.0 to 9.2. Of the amino acids tested, none could replace glutamine in the transamination reaction. Glyoxylate and phenylpyruvate was found to be the best amino acceptors. The Km values for glutamine and glyoxylate were 0.6 and 1.5 mM, respectively.

Mentioned in this Paper

Polyacrylamide Gels
Amino Acids, I.V. solution additive
Pyridoxal Phosphate
Sulfhydryl Reagents
Spectrophotometry, Ultraviolet
Metabolic Inhibition

About this Paper

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