Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1993-10-19
pubmed:abstractText
Rat 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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0145-5680
pubmed:author
pubmed:issnType
Print
pubmed:volume
39
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
469-77
pubmed:dateRevised
2003-11-14
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
Stabilization of phospho-intermediates of rat liver plasma membrane alkaline phosphatase by uncompetitive inhibition. Relation with phosphate uptake into hepatocytes.
pubmed:affiliation
Groupe de Recherche et d'Etude d' Analogues de Médicaments, Faculté de Médecine et de Pharmacie, Poitiers, France.
pubmed:publicationType
Journal Article