Enzymatic methyl esterification of specific glutamyl residue in corticotropin.
AUTOR(ES)
Kim, S
RESUMO
Ovine corticotropin (alpha s-ACTH) was enzymatically methylated with purified calf brain protein methylase II (protein O-methyltransferase; S-adenosyl-L-methionine: protein-carboxyl O-methyltransferase, EC 2.1.1.24) and S-adenosyl-L-[methyl-14C]methionine. After incubation for 60 min at 37 degrees C, 30 mol % of the hormone was methylated on the basis of the [14C]methyl incorporation. In order to assess the location of methylation, the modified peptide was digested with pepsin. Analytical results derived from studies on the peptic digest led to the suggestion that the alpha s-ACTH-(6--28) peptide fragment was esterified. Because there is only one available methylation site at Glu-28, these results indicate that Glu-28 of alpha s-ACTH was specifically methyl esterified to yield [Glu(OMe)28]-alpha s-ACTH.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=411551Documentos Relacionados
- Enzymatic methyl esterification of Escherichia coli ribosomal proteins.
- Transcriptional regulation of steroid hydroxylase genes by corticotropin.
- Role of adrenal renin in the regulation of adrenal steroidogenesis by corticotropin.
- PRODUCTION OF METHYL ESTERS BY ENZYMATIC HYDROESTERIFICATION OF CHICKEN FAT INDUSTRIAL RESIDUE
- Adrenal cholesterol uptake from plasma lipoproteins: regulation by corticotropin.
