Evidence that the hydrophobic domain of rat renal γ-glutamyltransferase spans the brush border membrane
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Biochemistry,Biophysics
Reference34 articles.
1. γ-Glutamyltransferase in kidney brush border membranes
2. Identity of maleate-stimulated glutaminase with gamma-glutamyl transpeptidase in rat kidney.
3. Comparison of the size and physical properties of gamma-glutamyltranspeptidase purified from rat kidney following solubilization with papain or with Triton X-100
4. Comparison of the association and orientation of gamma-glutamyltranspeptidase in lecithin vesicles and in native membranes.
5. gamma-Glutamyl Transpeptidase: Sidedness of Its Active Site on Renal Brush-Border Membrane
Cited by 5 articles. 订阅此论文施引文献 订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献
1. Glutathione metabolism and its selective modification.;Journal of Biological Chemistry;1988-11
2. Uses of γ-Glutamyltransferase in Experimental Toxicology;Advances in Veterinary Science and Comparative Medicine;1987
3. [50] γ-Glutamyl transpeptidase from kidney;Glutamate, Glutamine, Glutathione, and Related Compounds;1985
4. Immunocytochemical localization of γ-glutamyl-transferase on isolated renal cortical tubular fragments;Histochemistry;1984-05
5. Processing of the propeptide form of rat renal γ-glutamyltranspeptidase;FEBS Letters;1983-06-27
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