[Study of the amino acid composition of albumin fractions obtained from human serum albumin].

Six fractions were isolated from the commercial lyophised albumin preparation by the method of deposition in the medium of 3M KCl. The fractions were purified by means of preparative disc electrophoresis from globulins and polymers, and their amino acid composition was studied on the analyser KLA-3B. The significant differences (p=0.001) are found by lysine, ammonia, histidine, arginine, threonine, glutaminic acid, and phenyl alanine. The greatest differences are found by lysine, ammonia, glutaminic acid and phenylalanine. The fraction was also found being 9% of the initial albumin and sharply differing from the rest of the fractions in amino acid composition but identical immunologically. It is supposed that albumin heterogeneity is connected both with the presence of molecular forms differing in the primary structure and with different degree of amidation of glutaminic and aspartyl residues.