Activation of kidney prorenin by kidney cathepsin B isozymes.
Kidney protein was converted to a form of active renin by kidney cathepsin B isozymes. The three isozymes showed similar catalytic behavior for prorenin. The optimal pH for the activation was in the range of 4.0-5.0 and the reaction was completely inhibited by leupeptin. The molecular weight and the isoelectric point of the activated prorenin were 40,000 and pH 4.9. As a minor product, an activated prorenin having an isoelectric point of 5.2 was also produced.
D000818:Animals; D002401:Cathepsin B; D002403:Cathepsins / Q000494:pharmacology*; D004789:Enzyme Activation / Q000187:drug effects; D004792:Enzyme Precursors / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D007526:Isoelectric Point; D007527:Isoenzymes / Q000494:pharmacology*; D007668:Kidney / Q000201:enzymology*; D007976:Leupeptins / Q000494:pharmacology; D008970:Molecular Weight; D012083:Renin / Q000378:metabolism*; D013552:Swine
D004792:Enzyme Precursors; D007527:Isoenzymes; D007976:Leupeptins; D002403:Cathepsins; D002401:Cathepsin B; D012083:Renin