Literature DB >> 15625882

The effects of ligands on enzymic carboxyl-methylation of neurophysins.

E J Diliberto1, J Axelrod, I M Chaiken.   

Abstract

The methyl-acceptor activities of bovine neurophysins I and II for the enzyme protein carboxymethylase (EC 2.1.1.24) were found to be similar and as high as for other previously identified, biologically active protein substrates. Effects on the rate of methylation of these neurophysins were investigated with the posterior pituitary hormone ligands, oxytocin and vasopressin, and the hormone-related tripeptide ligand, methionyl-tyrosyl-phenylalaninamide. An increase in the rate of neurophysin II methylation was observed with both oxytocin and tripeptide. This ligand-induced response did not occur with either native neurophysin I or disulfide-scrambled neurophysin II.

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Year:  1976        PMID: 15625882     DOI: 10.1016/0006-291x(76)90231-x

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN: 0006-291X            Impact factor:   3.575


  2 in total

1.  A protein methylesterase involved in bacterial sensing.

Authors:  J B Stock; D E Koshland
Journal:  Proc Natl Acad Sci U S A       Date:  1978-08       Impact factor: 11.205

2.  The localization of protein carboxyl-methylase in sperm tails.

Authors:  P Bouchard; C Gagnon; D M Phillips; C W Bardin
Journal:  J Cell Biol       Date:  1980-08       Impact factor: 10.539

  2 in total

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