Urinary alkaline phosphatase: inhibition and electrophoresis characteristics
Cornell, A.E.; Hodson, A.W.
Medical Laboratory Sciences 38(3): 171-176
1981
ISSN/ISBN: 0308-3616 PMID: 7038365 Document Number: 182481
Inhibition by L-phenylalanine, L-homoarginine, heat and urea were measured to identify the source of urinary alkaline phosphatase. The inhibition patterns in urine from pregnant women, persons with bone or liver disease and normal persons, were similar and different from those of other human and Escherichia coli alkaline phosphatases. Kidney and urinary enzymes were similar. Using gradient-pore electrophoresis the urinary and bacterial enzymes and an isoenzyme in kidney had similar MW. With starch gel electrophoresis this kidney isoenzyme and the urinary enzyme had the same charge, but that of the bacterial enzyme was different.