[Methylation of ribonuclease and albumin by methyl cobalamin].

The capacity of methyl cobalamine (14CH3-B12) to methylate RNase and albumin in in vitro systems was studied. Under the experimental conditions, 14CH3-B12 methylated proteins about 100--1000 times more actively than S-adenosyl-methionine, a universal donor of methyl groups. The nature of buffer and pH 2 to 8 had no noticeable effect on the methylating capacity of 14CH3-B12. However, at higher pH rate of incorporation of methyl groups slightly increased. The 14CH3-groups incorporated into RNase amino acids remained stable upon illumination, in the presence of KCN in the incubation medium, and when heated in 20% HCl for 24--72 hr at 105 degrees. Methylation did not influence the enzymic properties of RNase. The automatic amino acid analyzer showed three peaks of the label of modified amino acids in the hydrolzates of methylated RNase, one of which corresponded to methylated methionine.