Calmodulin in human serum and the specific release of calmodulin from calmodulin-rich platelets
- 1 August 1984
- journal article
- research article
- Published by Portland Press Ltd. in Bioscience Reports
- Vol. 4 (8), 643-650
- https://doi.org/10.1007/bf01121017
Abstract
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.This publication has 17 references indexed in Scilit:
- Effect of exogenous calmodulin on lymphocyte proliferation in normal subjectsBulletin of Experimental Biology and Medicine, 1983
- Ca2+-induced hydrophobic site on calmodulin: Application for purification of calmodulin by phenyl-Sepharose affinity chromatographyBiochemical and Biophysical Research Communications, 1982
- Modulation of platelet shape and membrane receptor binding by Ca2+–calmodulin complexNature, 1981
- Involvement of calmodulin in platelet reactionThrombosis Research, 1981
- Calmodulin stimulates DNA synthesis by rat liver cellsBiochemical and Biophysical Research Communications, 1980
- Platelet phosphorylase kinase activity and its regulation by the calcium-dependent regulatory protein, calmodulinBiochimica et Biophysica Acta (BBA) - Enzymology, 1980
- Calmodulin Plays a Pivotal Role in Cellular RegulationScience, 1980
- Human platelet myosin light chain kinase requires the calcium-binding protein calmodulin for activity.Proceedings of the National Academy of Sciences, 1979
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970