Isolation and characterization of human blood platelet gelsolin
- 20 August 1984
- journal article
- Published by Wiley in FEBS Letters
- Vol. 174 (1) , 80-85
- https://doi.org/10.1016/0014-5793(84)81082-0
Abstract
A 90‐kDa protein‐actin stable complex was purified from blood platelets by a short and efficient procedure giving at the same time actin used in polymerization assays. 90‐kDa protein free of actin was prepared from the complex by 8 M ureau treatment and renaturation. By its molecular mass, immunological cross‐reactivity with macrophage gelsolin and its effect on G‐ and F‐actin the 90‐kDa protein appears as the platelet gelsolin.Keywords
This publication has 24 references indexed in Scilit:
- Polymorphism of α‐actinin from human blood platelets Homodimeric and heterodimeric formsEuropean Journal of Biochemistry, 1984
- Muscle gelsolin: isolation from heart tissue and characterization as an integral myofibrillar proteinFEBS Letters, 1984
- A Ca2+‐dependent actin modulator from vertebrate smooth muscleFEBS Letters, 1984
- ‘Cap 90’, a 90‐kDa Ca2+‐dependent F‐actin‐capping protein from vertebrate brainFEBS Letters, 1983
- A 90 000-dalton actin-binding protein from platelets comparison with villin and plasma brevinBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1982
- Comparison of the properties of two kinds of preparations of human blood platelet actin with sarcomeric actinBiochimie, 1982
- F actin assembly modulated by villin: Ca++-dependent nucleation and capping of the barbed endCell, 1981
- 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