[Characteristics of the molecular diversities of human and rat aldolase via starch and agar gel electrophoresis].

Content of aldolase isoenzymes was reinvestigated in human and rat tissues by means of agar and starch gel electrophoresis. Heterogeneity of the A type aldolase is established and possible causes of formation of the multiple forms of the enzyme are discussed. The ratio of various fractions of aldolase A was different in erythrocytes of newborn and aldult persons. The patterns of the aldolase isozyme spectra were characterized in blood sera of newborns, in acute hepatitis and myocardial infarction.