ロイシンデヒドロゲナーゼを共役させたヒトアミノペプチダーゼの定量的活性染色法

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  • A quantitative staining method for human aminopeptidases using leucine dehydrogenase as coupling enzyme

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An electrophoretic separation and a quantitative staining method for leucine aminopeptidase, arylamidase and cystyl aminopeptidase were described. L-Leucinamide was used as a substrate for the aminopeptidases electrophoretically separated, and the liberated L-leucine was oxidized by leucine dehydrogenase and NAD+. The activity bands were visualized by tetrazolium salt (MTT) as a final hydrogen acceptor.<br>Arylamidase and cystyl aminopeptidase were stained in the area of pre α1- and between α1 and α2-globulin position, respectively. The leucine aminopeptidase was samely stained in the area of pre β-globulin. Employing this method, it was possible to determine the activity of each aminopeptidase with satisfactory accuracy and reproducibility.<br>Furthermore, this method would be useful to the analysis of enzymological properties of aminopeptidases because of its availability to other peptides, such as L-leucylglycine and L-leucyl-L-leucine, as substrate.

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