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- W2078334808 abstract "A steady-state kinetic analysis of the activation of bovine Factor X, by bovine Factor Xa, was undertaken. The activation was found to be dependent on the presence of divalent cations; Ca2+ showing the greatest stimulatory effect and Mn2+ exhibiting a lower degree of activity for this reaction. Although Sr2+ and Mg2+ were ineffective when present alone, each contributed synergistically to the activation rate at suboptimal levels of Ca2+. The effect of phospholipid (phosphatidylcholine:phosphatidylserine, 4:1, w:w) on the rate of activation and on the activation pathway was investigated. Phospholipid (PL) concentrations of up to 40 μm had no effect on the activation rate; whereas, concentrations of 40–180 μm were slightly inhibitory. In the absence of PL, the major product of the activation was Factor α-Xa, while in the presence of PL, lower-molecular-weight forms of Factor X (Factor β-X) and Factor Xa (Factor β-Xa were produced. At saturating levels of Ca2+, the Km app for the activation, at pH 7.4 and 37 °C, in the absence of PL, was found to be 0.6 ± 0.1 μm and the V was 1.7 ± 0.3 mol Factor X cleaved min−1 mol−1 Factor Xa. The corresponding values, in the presence of 90 μm PL, were 1.4 ± 0.2 μm and 2.2 ± 0.2 mol Factor X cleaved min−1 mol−1 Factor Xa." @default.
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- W2078334808 date "1982-04-01" @default.
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- W2078334808 title "The activation of bovine Factor X by bovine Factor Xa" @default.
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- W2078334808 doi "https://doi.org/10.1016/0003-9861(82)90297-1" @default.
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