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The inhibitory properties of levamisole and its analogue R 8231 on alkaline phosphatases of various rat tissues were investigated cytochemically. Very low concentrations, respectively, 0.5 and 0.1 mM, sufficed to achieve complete inhibition in most tissues except intestine. The inhibition was reversible as for other known uncompetetive inhibitors but was found to be substrate-independent. The influence of fixation and incubation procedures was negligable. Other phosphatases as acid phosphatase, adenosine triphosphatase, thiamine pyrophosphatase, glucose 6-phosphatase and 5'-nucleotidase remained unchanged in the presence of the inhibitors.
Μ. Borgers (Sat,) studied this question.