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ATPases (Adenosine Triphosphatases) are enzymes that hydrolyze ATP to obtain energy and perform some type of work in the cell. This article characterized the ATPasic activity of a fraction obtained from bovine brain using the rat brain myosin V protocol. The fraction obtained showed high ATPásica activity with Mg (100%) and Co (95%). Lower values were found with calcium (50%), zinc (40%), copper (15%) and iron (10%). The kinetic curves of cation concentration suggest that the catalytic site of the enzyme in question does not distinguish the cation-ATP complex. Tests with Mg, Co and Mg/Co resulted in nearly equal ATPasic activities, which rules out the presence of distinct enzymes. The enzymatic behavior of this fraction is different from that described in the original method, indicating that the enzyme found in the rat brain fraction (myosin V) is different from the enzyme found in ox brain, or just that its catalytic site works in a different way from first.

CARACTERIZAÇÃO DE UMA FRAÇÃO RICA EM ATIVIDADE COBALTO-ATPÁSICA DE CÉREBRO BOVINO