Quantitative method for determining serum alkaline phosphatase isoenzyme activity I. Guanidine hydrochloride: New reagent for selectively inhibiting major serum isoenzymes of alkaline phosphatase

M. D.S. Shephard, M. J. Peake

Research output: Contribution to journalArticle

19 Citations (Scopus)

Abstract

The potential use of the protein denaturant guanidine hydrochloride to inhibit selectively the enzyme activity of serum alkaline phosphatase isoenzymes from liver, bone, intestine, and placenta was investigated. Inhibition of each isoenzyme was shown to be dependent on time and concentration of inhibitor. In the presence of 0.3 mol/l (28.7 g/l) guanidine hydrochloride for 170 seconds 14%, 47%, and 90% of the total alkaline phosphatase activity remained in samples of bone, liver, and intestinal origins, respectively. In contrast, the activity of the placental isoenzyme increased by 24%. The degree of inhibition was shown to be independent of total alkaline phosphatase activity. Investigations were performed at 37°C using the Cobas Bio centrifugal analyser. We conclude that this reagent has several practical advantages over urea as a selective inhibitor of alkaline phosphatase isoenzymes, including a faster and more reproducible inhibition at a much lower reagent concentration.

Original languageEnglish
Pages (from-to)1025-1030
Number of pages6
JournalJournal of Clinical Pathology
Volume39
Issue number9
DOIs
Publication statusPublished - 1 Sep 1986
Externally publishedYes

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