caa a22 4500 469094184 CHVBK 20180323133026.0 cr unu---uuuuu 170328e19921201xx s 000 0 eng 10.1007/BF02576285 doi (NATIONALLICENCE)springer-10.1007/BF02576285 Changes in membrane-bound hydrolases by metronidazole in rat renal brush border [Elektronische Daten] [Leelank Jamba, Shankar Sanyal] Summary: The antiprotozoal drug metronidazole, when administered orally at a dose level of 100 mg/kg body wt. daily for 7 days to rats, brought about significant elevation of renal brush-border-membrane-bound hydrolytic enzymes, such as alkaline phosphatase, maltase, sucrase, and leucine aminopeptidase (LAP). Kinetic analysis of the enzymes (substrate saturation) indicated that the drug produced an increase in the maximum of apparent initial enzyme velocity (V max), while the substrate affinity constant (K m) remained unaltered. These changes were not recovered to the normal level event after the drug regimen was stopped and the animals were allowed to recover for a period of 7 days. Lipid analysis of brush border membrane (BBM) revealed a significant elevation in the cholesterol, phospholipid, and ganglioside levels, while no marked change was recorded in triglyceride, free fatty acid and plasmalogen. Study of the temperature-dependent parameters of the enzymes showed that metronidazole induced a shift in the transition temperature (T o) in LAP with nearly total reversibility in the recovery group. No such change was seen in the other enzymes. However, there also was a lowering in the energy of activation (E a) belowT o, which returned to normal after the treatment was withdrawn. Springer-Verlag, 1992 Metronidazole nationallicence Renal brush border membrane nationallicence Hydrolytic enzymes nationallicence Lipids nationallicence Jamba Leelank Department of Biophysics, Panjab University, 160014, Chandiagrh, India aut Sanyal Shankar Department of Biophysics, Panjab University, 160014, Chandiagrh, India aut Research in Experimental Medicine Springer-Verlag 192/1(1992-12-01), 287-294 0300-9130 192:1<287 1992 192 433 https://doi.org/10.1007/BF02576285 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/BF02576285 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Jamba Leelank Department of Biophysics, Panjab University, 160014, Chandiagrh, India aut NATIONALLICENCE 700 1- Sanyal Shankar Department of Biophysics, Panjab University, 160014, Chandiagrh, India aut NATIONALLICENCE 773 0- Research in Experimental Medicine Springer-Verlag 192/1(1992-12-01), 287-294 0300-9130 192:1<287 1992 192 433 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer