par Polastro, Enrico 
;Deconinck, Marc Melchior ;Devogel, Myriam ;Mailier, E.L.;Looza, Y.B.;Schnek, Arthur Georges ;Leonis, José
Référence Biochemical and biophysical research communications, 81, 3, page (920-927)
Publication Publié, 1978-04
;Deconinck, Marc Melchior ;Devogel, Myriam ;Mailier, E.L.;Looza, Y.B.;Schnek, Arthur Georges ;Leonis, José Référence Biochemical and biophysical research communications, 81, 3, page (920-927)
Publication Publié, 1978-04
Article révisé par les pairs
| Résumé : | Protein methylase II (S-adenosyl-L-methionine: protein carboxyl-O-methyltransferase; E.C. 2.1.1.24) has been purified 28 000 fold from equine erythrocytes. The purified enzyme is homogeneous on polyacrylamide gel electrophoresis performed either in presence or in absence of SDS, and on analytical ultracentrifugation. It appears constituted of a single polypeptidic chain of a molecular weight very close to 25 000 Daltons. Other enzymatic properties of the protein are quite similar to those previously reported for similar enzymes. The amino acid analysis of the enzyme is presented. The single cysteine residue, the enzyme contains, is essential for the enzymatic activity. Other amino acids apparentely involved in catalysis are tentatively identified. © 1978. |
