Calmodulin(CaM)-like activity was detected in human serum and foetal calf serum, with an activity i0 times more than that detectable in plasma. Serum CaM was largely accounted for by release from human platelets as confirmed by both radioimmunoassay and sodium-dodecyl-sulphate/polyacrylamide-gel electrophoresis of CaM partially purified from platelet releasate obtained in response to thrombin. Lactate dehydrogenase release was unaffected by thrombin. Platelet CaM content was very variable (1.3 to 11.3 pg/mg protein; n = 15). It is suggested that intact platelets are rich in CaM and that release of CaM during preparation explains the variation in CaM content reported here and in the literature.
Calmodulin in human serum and the specific release of calmodulin from calmodulin-rich platelets
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Sheila Mac Neil, Simon W. Walker, Janet Seid, Stephen Tomlinson; Calmodulin in human serum and the specific release of calmodulin from calmodulin-rich platelets. Biosci Rep 1 August 1984; 4 (8): 643–650. doi: https://doi.org/10.1007/BF01121017
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