Proteolytic activity in mouse urine: relationship to the kidney metallo-endopeptidase, meprin.
Meprin, a brush border kidney metallo-endopeptidase is present as the major endopeptidase in mouse urine. The enzyme is freely soluble and can be detected enzymically or immunologically. Mice can be partitioned into two phenotypes that differ by 10-20-fold in the amount of meprin in kidney membranes; this phenotypic variation is reflected in urinary activities. We propose a role for meprin in the degradation of other urinary proteins.
Flannery
A V
AV
Department of Biochemistry, University of Liverpool, U.K.
Dalzell
G N
GN
Beynon
R J
RJ
D000818:Animals; D015153:Blotting, Western; D004591:Electrophoresis, Polyacrylamide Gel; D010450:Endopeptidases / Q000302:isolation & purification / Q000652:urine*; D006020:Glycopeptides / Q000494:pharmacology; D007328:Insulin; D007668:Kidney / Q000201:enzymology*; D007700:Kinetics; D008666:Metalloendopeptidases / Q000378:metabolism* / Q000652:urine; D051379:Mice; D008815:Mice, Inbred Strains; D011480:Protease Inhibitors / Q000494:pharmacology; D013379:Substrate Specificity
D006020:Glycopeptides; D007328:Insulin; D011480:Protease Inhibitors; D010450:Endopeptidases; D008666:Metalloendopeptidases; C053833:meprin A; C008890:phosphoramidon