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pubmed-article:8374502pubmed:abstractTextRat liver plasma membrane alkaline phosphatase (ALP) phospho-intermediates, which have molecular masses of 151 and 135 kDa bands, were labelled at physiological pH with either (gamma-32P) ATP or 32Pi. This labeling was stabilized by a potent enzyme inhibitor, bromolevamisole (BL), and not by bromodexamisole (BD). BL augmented the rate and extent of autophosphorylation and slowed down the rate of autodephosphorylation of ALP. The phospho-intermediates labeling presented nearly the same kinetic behaviour with either (gamma-32P) ATP or 32Pi. In the presence of BL a marked decrease of the phosphorylation state of many proteins was observed in hepatocytes. BL also produced a decrease of the 32Pi uptake into hepatocytes and a decrease of the specific radioactivity of cellular ATP. BD had nearly the same effect as BL on protein phosphorylation and 32Pi uptake. These results argued against a direct involvement of ALP in Pi transport across hepatocyte plasma membrane.lld:pubmed
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pubmed-article:8374502pubmed:articleTitleStabilization of phospho-intermediates of rat liver plasma membrane alkaline phosphatase by uncompetitive inhibition. Relation with phosphate uptake into hepatocytes.lld:pubmed
pubmed-article:8374502pubmed:affiliationGroupe de Recherche et d'Etude d' Analogues de Médicaments, Faculté de Médecine et de Pharmacie, Poitiers, France.lld:pubmed
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