[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.
D000328:Adult; D000818:Animals; D004796:Clinical Enzyme Tests / Q000379:methods; D004586:Electrophoresis / Q000379:methods; D004587:Electrophoresis, Agar Gel / Q000379:methods; D004592:Electrophoresis, Starch Gel / Q000379:methods; D004789:Enzyme Activation; D005634:Fructose-Bisphosphate Aldolase / Q000032:analysis*; D006801:Humans; D007231:Infant, Newborn; D007527:Isoenzymes / Q000032:analysis; D008967:Molecular Biology; D051381:Rats
D007527:Isoenzymes; D005634:Fructose-Bisphosphate Aldolase
Kharakteristika molekuliarnykh raznovidnosteĭ al'dolazy cheloveka i krysy s pomoshch'iu élektroforeza na krakhmal'nom i agarovom geliakh.