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Neurochemical Research

, Volume 9, Issue 7, pp 927–934 | Cite as

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

  • Jaroslav Veselý
  • Miroslav Černoch
Original Articles

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.

Keywords

Human Brain Deoxycholate Papain Choroid Plexus Sodium Deoxycholate 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Plenum Publishing Corporation 1984

Authors and Affiliations

  • Jaroslav Veselý
    • 1
  • Miroslav Černoch
    • 2
  1. 1.Institute of ChemistryPalacký University, Medical FacultyOlomoucCzechoslovakia
  2. 2.Research Institute of Clinical and Experimental OncologyBrnoČSSR

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