Solubilization and some properties of γ-glutamyltransferase from human brain microvessels
- 17 Downloads
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.
KeywordsHuman Brain Deoxycholate Papain Choroid Plexus Sodium Deoxycholate
Unable to display preview. Download preview PDF.
- 7.Meister, A., Tate, S. S., andRoss, L. L. 1976. Membrane-bound γ-glutamyl transpeptidase. Pages 315–347,in Martonosi, A. (ed.) The enzymes of biological membranes, Vol. 3, Membrane transport, Plenum Press, New York.Google Scholar
- 10.Lisý, V., andLodin, Z. 1977. In vitro influencing of brain γ-glutamyl transpeptidase activity by some amino acids. Collection Czechoslov. Chem. Commun. 42:2967–2974.Google Scholar
- 19.Veselý, J., andČernoch, M. 1984. Studies of γ-glutamyltransferase activity in the brain tissue post mortem. Neurochem. Res.Google Scholar
- 21.Kulhánek, V., andDimov, D. M. 1973. Bestimmung der γ-Glutamyltranspeptidase. Ergebnisse Exp. Med. 12:161–169.Google Scholar
- 25.Leibach, F. H., andBinkley, F. 1968. γ-Glutamyl transferase of swine kidney. Biochem. Z. 338:317–329.Google Scholar
- 27.Hughey, R. P., andCurthoys, N. P. 1976. Comparison of the size and physical properties of γ-glutamyltranspeptidase purified from rat kidney following solubilization with papain or with Triton X-100. J. Biol. Chem. 251:7863–7820.Google Scholar