Neurochemical Research

, Volume 10, Issue 10, pp 1325–1334 | Cite as

Partial purification of γ-glutamyltransferase from human brain microvessels

  • Jaroslav Veselý
  • Václav Lisý
  • Miroslav Černoch
Original Articles


Two forms of gamma-glutamyltransferase from human brain cortex microvessels were partially purified by gel permeation and ion-exchange and group-affinity chromatography. The specific activity of the purified preparations was 320-fold (detergent form) and 830-fold (proteolytic form) higher than that of the enzyme in the brain cortex homogenate. The relative molecular mass of the proteolytic form of the enzyme was about 90,000 as determined by gel permeation chromatography. The major part of the enzyme (about 80%) was absorbed on Con A-Sepharose 4B. The pH optima for transfer reactions with γ-glutamyl-4-nitroanilide as donor and glycylglycine andl-cystine as acceptors were in the range of 8.2 to 9.0. The studied enzyme was inhibited by a mixture ofl-serine and borate and by bromcresol green.


Human Brain Borate Brain Cortex Partial Purification Relative Molecular Mass 
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Copyright information

© Plenum Publishing Corporation 1985

Authors and Affiliations

  • Jaroslav Veselý
    • 1
  • Václav Lisý
    • 2
  • Miroslav Černoch
    • 1
  1. 1.Institute of ChemistryPalacký University Medical FacultyOlomoucCzechoslovakia
  2. 2.Institute of PhysiologyCzechoslovak Academy of SciencesPragueCzechoslovakia

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