Abstract
1. Rat kidneys which were perfused with saline contained both kininogenase (KGA) and kininase activity. These activities were separated by gel filtration on a Sephadex G-100 column. The kininase activity was excluded from the column whereas the KGA activity was retained. Kidney KGA activity was primarily found in the sedimentable fraction of the homogenate.2. The kidney KGA activity was compared with the urinary KGA activity, and the following properties were found to be the same: molecular dimension, pH optimum, effect of inhibitors, and ability to liberate kinins from kininogens.3. A urinary sample collected over 24 h contained about 8 times the KGA activity found in the corresponding kidneys at the end of the collection period. The urine: kidney ratio for alkaline phosphatase was about 0.01.4. The ability of kidney and urinary samples to hydrolyse N-alpha-benzoyl-L-arginine ethyl ester (BAEE) at pH 8.5 paralleled the KGA activity.
MeSH Terms
Alkaline Phosphatase/analysis,urine
Animals
Chromatography, Gel
Endopeptidases/urine
Esters/metabolism
Female
Hydrogen-Ion Concentration
In Vitro Techniques
Kallikreins/urine
Kidney/enzymology
Kinins/blood,metabolism
Male
Molecular Weight
Rats
Tissue Extracts
Chemicals
Esters
Kinins
Tissue Extracts
Alkaline Phosphatase
Endopeptidases
Kallikreins
Authors & Affiliations
1 authors, click to expand affiliations / ORCID
Nustad K
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