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  • Title: Phosphorylated proteins from anuran intestinal microvilli membranes--I. Relations with alkaline phosphatase.
    Author: el Maraghi-Ater H, Hourdry J, Mesnard J, Dupuis Y.
    Journal: Comp Biochem Physiol B; 1986; 83(2):415-23. PubMed ID: 3485510.
    Abstract:
    The degree of phosphorylation of intestinal microvilli membrane proteins in an adult amphibian, Rana esculenta, was investigated under various experimental conditions. The microvilli protein phosphorylation rate rapidly increases during the first 4 min of incubation in a medium containing [gamma-32P]ATP. This increase is slower afterwards. Cyclic nucleotides (cyclic AMP, cyclic GMP) and sorbitol do not modify the microvilli protein phosphorylation rate. On the contrary, this phosphorylation rate significantly decreases in the presence of L-lysine, when its concentration in the incubation medium is greater than 25 mM. The time course of phosphorylation confirms the inhibitory effects of L-lysine (100 mM). The microvilli membrane proteins were distinguished by polyacrylamide gel electrophoresis. In heated samples, electrophoresis followed by an radioautograph systematically reveals the existence of a very phosphorylated protein with a mol. wt of 86 kDa. The phosphorylation of this protein is partially inhibited by L-lysine (100 mM). The very phosphorylated protein could be the monomer of alkaline phosphatase. The dimer (170 kDa) is visualized on electrophoretograms by its catalytic activity. In mammals, several authors have established a correlation between phosphorylation of the microvilli membrane proteins and the intensity of intestinal calcium absorption. Such a control is presently being investigated in adult Rana esculenta.
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