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- W1588611036 abstract "At low concentrations of ATP glycerinated cilia swell, as indicated by an increase in packed volume after low speed centrifugation. At high concentrations of ATP partial dissolution occurs. The soluble proteins thus obtained were resolved by sucrose density gradient sedimentation. Three major peaks were obtained: a nonadenosine triphosphatase protein sedimenting at 4 S; an ATPase of low specific activity sedimenting at 14 S; and an ATPase of high specific activity and high substrate specificity sedimenting at 30 S. The pellet remaining after extraction contained ciliary membranes and outer fiber pairs, and had ATPase activity of low specific activity and low substrate specificity. After extraction with high ATP the residual pellet no longer swelled in response to the addition of a low concentration of ATP. The 30 S protein can recombine functionally with the pellet, as judged by an increase in turbidity which could be reversed by the addition of ATP. The low specific activity, 14 S ATPase is activated by ethylenediaminetetraacetic acid, but the 30 S ATP is not. Both ATPases are activated by Mg++ and by Ca++. The fractions obtained by this method resemble those obtained by Gibbons from ethanol- and calcium-isolated cilia by his fractionation procedure." @default.
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- W1588611036 date "1969-01-01" @default.
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- W1588611036 title "The Fractionation of Glycerinated Cilia by Adenosine Triphosphate" @default.
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- W1588611036 doi "https://doi.org/10.1016/s0021-9258(18)94440-6" @default.
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