[Isolation and primary characterization of two forms of inorganic pyrophosphatase from ox heart muscle mitochondria].
A method allowing to obtain two highly purified forms (membrane-bound and soluble ones) of inorganic pyrophosphatase from bovine heart mitochondria is described. Both forms have the isoelectric point of 5.8, pH optimum with Mg2+ at 7--9, are maximally stable at pH 5.8 and absolutely specific to PPi and require Mg2+ or Co2+ for their activity. The soluble pyrophosphatase is also activated by Zn2+. Besides, the two forms differ in their electrophoretic mobilities, affinity for DEAE cellulose and stability in acidic (pH less than 5.8) and alkaline media.
D000818:Animals; D002417:Cattle; D003035:Cobalt / Q000494:pharmacology; D004789:Enzyme Activation; D043564:Inorganic Pyrophosphatase; D007527:Isoenzymes / Q000302:isolation & purification / Q000378:metabolism; D007700:Kinetics; D008274:Magnesium / Q000494:pharmacology; D008297:Male; D008929:Mitochondria, Heart / Q000201:enzymology*; D011755:Pyrophosphatases / Q000302:isolation & purification / Q000378:metabolism*; D015032:Zinc / Q000494:pharmacology
D007527:Isoenzymes; D003035:Cobalt; D011755:Pyrophosphatases; D043564:Inorganic Pyrophosphatase; D008274:Magnesium; D015032:Zinc
Vydelenie i pervichnaia kharakteristika dvukh form neorganicheskoĭ pirofosfatazy iz mitokhondriĭ serdechnoĭ myshtsy byka.