Abstract
Gamma-glutamyl transpeptidase was purified 53 times from Sheep brain cortex capillaries. On gel filtration it appears homogeneous with a M.W. = 350 000. The enzyme is likely a glycoprotein, the properties of which are close to hog kidney gamma-glutamyl transpeptidase ; gamma-glutamyl aminoacid formation is assayed electrophoretically. The results obtained using several aminoacids are in favour of the existence of different units, specific of each group of aminoacids ; together with the data from structural analogs, they support the hypothesis that gamma-glutamyl transpeptidase participates in aminoacid transport accross blood brain barrier.
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