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• W2007928131 abstract "Isolated porcine platelet α granules display a Mg2+-stimulated ATPase activity. The enzyme is membrane bound and several criteria suggest that it is intrinsic to the α granules, rather than arising from contamination with other structures. Characterization of the ATPase revealed an apparent Km for ATP of 198 μm. Other nucleotides are also hydrolyzed by the enzyme, though at a slower rate. The enzyme has an absolute requirement for divalent cations, and both Mg2+ (apparent Km 0.93 mm) and Ca2+ (apparent Km 0.95 mm) can activate it. Maximal hydrolysis rates are higher with Mg2+ than with Ca2+. Micromolar Ca2+ in the presence of maximally stimulating Mg2+ concentrations produces a small additional enhancement of activity. The Mg2+ ATPase has a broad activity maximum between pH 6.5 and 8.5, and an activation energy of 11.8 Kcal/mol. Several independent observations suggest that the ATPase could be involved in H+ translocation across the granule membrane: (a) the activity is stimulated upon disrupting membrane continuity by either hypotonic lysis or addition of nondenaturing detergents; (b) proton ionophores enhance the activity in intact but not in disrupted α granules; (c) permeating anions stimulate the ATPase more than slowly permeant or impermeant ones; (d) addition of NH3 (as either NH4Cl or (NH4)2SO4) activates enzyme activity; (e) silicotungstate and disulfonic stilbene derivatives, which are inhibitors of other H+-transporting ATPases, also inhibit the α-granule enzyme. These findings are compared with the reported properties of H+ pumps of other storage and secretory organelles." @default.
• W2007928131 created "2016-06-24" @default.
• W2007928131 creator A5062437833 @default.
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• W2007928131 date "1982-10-01" @default.
• W2007928131 modified "2023-10-16" @default.
• W2007928131 title "A Mg2+-stimulated ATPase in platelet α-granule membranes: Possible involvement in proton translocation" @default.
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• W2007928131 doi "https://doi.org/10.1016/0003-9861(82)90374-5" @default.
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