Some properties of spectrin-like proteins from Pisum sativum.
Proteins cross-reacting with antibodies directed against alpha- and beta-spectrin were recently detected in plant cells. In this report we have studied the ability of these proteins to interact with other components of membrane skeleton such as ankyrin, f-actin and calmodulin. It was found that the polypeptide of high molecular weight reacting with anti-alpha-spectrin antibody binds calmodulin in Ca(2+)-dependent manner. Protein complexes containing polypeptides cross-reacting with anti-spectrin antibodies interact with muscle f-actin (in co-sedimentation assay) and with erythrocyte ankyrin (ELISA-type assay). These data further substantiate a possibility of occurrence of spectrin-based membrane skeleton in higher plant cells.
Bisikirska
B
B
University of Wrocław, Department of Genetic Biochemistry, Poland.
Sikorski
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AF
D000199:Actins / Q000378:metabolism; D000818:Animals; D017487:Ankyrins / Q000378:metabolism; D000906:Antibodies; D002147:Calmodulin / Q000378:metabolism; D003429:Cross Reactions; D004797:Enzyme-Linked Immunosorbent Assay; D004912:Erythrocytes / Q000378:metabolism; D008970:Molecular Weight; D018482:Muscle, Skeletal / Q000378:metabolism; D018532:Pisum sativum / Q000737:chemistry*; D010940:Plant Proteins / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism*; D011817:Rabbits; D013049:Spectrin / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism
D000199:Actins; D017487:Ankyrins; D000906:Antibodies; D002147:Calmodulin; D010940:Plant Proteins; D013049:Spectrin