Radiation inactivation probe of membrane-bound enzymes: γ-Glutamyltranspeptidase, aminopeptidase N, and sucrase
- 1 November 1986
- journal article
- research article
- Published by Elsevier in Analytical Biochemistry
- Vol. 158 (2) , 278-282
- https://doi.org/10.1016/0003-2697(86)90550-6
Abstract
No abstract availableKeywords
This publication has 23 references indexed in Scilit:
- Radiation target analysis of glycoproteinsAnalytical Biochemistry, 1986
- Assay of intestinal disaccharidasesScandinavian Journal of Clinical and Laboratory Investigation, 1984
- Processing of the propeptide form of rat renal γ‐glutamyltranspeptidaseFEBS Letters, 1983
- Multiple transport pathways for neutral amino acids in rabbit jejunal brush border vesiclesThe Journal of Membrane Biology, 1982
- Modification of the acceptor binding site of γ-glutamyl transpeptidase by the diazonium derivatives of p-aminohippurate and p-aminobenzoateArchives of Biochemistry and Biophysics, 1982
- Topology of microvillar membrance hydrolases of kidney and intestine.Physiological Reviews, 1982
- γ-Glutamyl transpeptidase: catalytic, structural and functional aspectsMolecular and Cellular Biochemistry, 1981
- Modulation of erythrocyte acetylcholinesterase by cardiolipin: Effect on subunit coupling revealed by irradiation inactivationBiochemical and Biophysical Research Communications, 1980
- Size determination of enzymes by radiation inactivationAnalytical Biochemistry, 1979
- γ-Glutamyl-p-nitroanilide: A new convenient substrate for determination and study of l- and d-γ-glutamyltranspeptidase activitiesBiochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects, 1963