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  • Title: Comparison of the structural characteristics of the 4-aminobutyrate:2-oxoglutarate transaminases from rat and human brain, and of their affinities for certain inhibitors.
    Author: Maitre M, Ciesielski L, Cash C, Mandel P.
    Journal: Biochim Biophys Acta; 1978 Feb 10; 522(2):385-99. PubMed ID: 623769.
    Abstract:
    4-Aminobutyrate:2-oxoglutarate (4-aminobutyrate:2-oxoglutarate amino-transferase, EC 2.6.1.19) from human brain has been purified 2500-fold with respect to the initial homogenate. The enzyme, which appears to be pure by polyacrylamide gel electrophoresis, N-terminal analysis and immunodiffusion, was compared to rat brain 4-aminobutyrate transaminase, purified to the same extent in an earlier study [15]. The two enzymes, which have approximately the same molecular weight, show large differences in their tryptic fingerprints and in the peptides produced by cyanogen bromide cleavage. The Km values (limit) for 4-aminobutyrate are different, the human enzyme having four times greater affinity for this substrate. A series of branched-chain fatty acids (including n-dipropylacetate), which are structural analogues of 4-aminobutyrate and inhibit rat brain 4-aminobutyrate transaminase, are less powerful inhibitors of the human enzyme.
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