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Solubilization and some properties of γ-glutamyltransferase from human brain microvessels

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Abstract

Detergents Triton X-100, sodium deoxycholate, and octyl-β-D-glucopyranoside, and proteinase papain proved to be excellent agents solubilizing the γ-glutamyl-transferase (γ-GT) from human brain cortex microvessels. Ficin also solubilized γ-GT but to a lesser extent than papain. The relative molecular mass of the detergent-solubilized enzyme form was greater than 200,000 (in the presence of Triton X-100). The relative molecular mass of the proteinase-solubilized form was slightly greater than that of albumine. γ-GTs of microvessels from five human brain regions and from the choroid plexus were tested for their specificity toward acceptors. The best acceptors were found to be (in decreasing order of activity)l-cystine, glycylglycine,l-glutamine,l-methionine, andl-alanine. The findings suggest that the main features of γ-GT of the human blood-brain barrier are very similar to those of γ-GTs from other human tissues.

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Author notes

  1. Miroslav Černoch

    Present address: Research Institute of Clinical and Experimental Oncology, Žlutý kopec 7, 602 00, Brno, ČSSR

Authors and Affiliations

  1. Institute of Chemistry, Palacký University, Medical Faculty, 775 15, Olomouc, Czechoslovakia

    Jaroslav Veselý

Authors
  1. Jaroslav Veselý
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  2. Miroslav Černoch
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Veselý, J., Černoch, M. Solubilization and some properties of γ-glutamyltransferase from human brain microvessels. Neurochem Res 9, 927–934 (1984). https://doi.org/10.1007/BF00964524

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