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Association of a myristoylated protein with a biological membrane and its increased phosphorylation by protein kinase C.
Utsumi, T; Yoshinaga, K; Koga, D; Ide, A; Nobori, K; Okimasu, E; Terada, S; Utsumi, K.
Afiliação
  • Utsumi T; Laboratory of Biological Chemistry, Faculty of Agriculture, Yamaguchi University, Japan.
FEBS Lett ; 238(1): 13-6, 1988 Sep 26.
Article em En | MEDLINE | ID: mdl-3169245
A hydrophilic enzyme, lysozyme, was myristoylated in vitro by the N-hydroxysuccinimide ester of myristic acid, and the monomyristoylated lysozyme was isolated by CM-cellulose cation-exchange column chromatography. The monomyristoylated lysozyme associated with phospholipid vesicles, whereas the association of native lysozyme was negligible. The membrane-associated monomyristoylated lysozyme was phosphorylated with partially purified rat brain Ca2+- and phospholipid-dependent protein kinase (protein kinase C) in the presence of Ca2+, phosphatidylserine and phorbolmyristate acetate. Thus, the myristoylated lysozyme became a substrate of protein kinase C through its hydrophobic association with the membrane. The present results suggest that the myristoylation of cytoplasmic proteins may have an important role in signal transduction.
Assuntos
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Base de dados: MEDLINE Assunto principal: Encéfalo / Proteína Quinase C / Muramidase / Lipoproteínas / Proteínas de Membrana / Ácidos Mirísticos Tipo de estudo: Risk_factors_studies Limite: Animals Idioma: En Revista: FEBS Lett Ano de publicação: 1988 Tipo de documento: Article País de afiliação: Japão
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Base de dados: MEDLINE Assunto principal: Encéfalo / Proteína Quinase C / Muramidase / Lipoproteínas / Proteínas de Membrana / Ácidos Mirísticos Tipo de estudo: Risk_factors_studies Limite: Animals Idioma: En Revista: FEBS Lett Ano de publicação: 1988 Tipo de documento: Article País de afiliação: Japão