Characterization and partial purification of a high-molecular-mass, calmodulin-binding, tyrosyl-phosphorylated protein from lymphocyte plasma membranes.
A plasma membrane phosphoprotein with a species-dependent molecular mass of 108 or 112 kDa (P108/112) was analyzed in lymphoid cells from rats and humans. After 24 h lectin stimulation its in vitro phosphorylation was raised to an important extent. Phosphotyrosine was analyzed by 2-D electrophoresis. Calmodulin was bound by P108/112 in a Ca2+-dependent manner. P108/112 remained insoluble after extraction with detergent, high salt, EDTA, or high pH. After chlorethanol extraction it was partially purified by gel filtration. P108/112 shows conspicuous similarities with the 110-kDa protein from chicken intestine microvilli.
Kostka
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Max Planck Institut für Biochemie, Martinsried, Federal Republic of Germany.
D000818:Animals; D002147:Calmodulin / Q000378:metabolism; D002148:Calmodulin-Binding Proteins / Q000032:analysis* / Q000302:isolation & purification / Q000378:metabolism; D003208:Concanavalin A / Q000494:pharmacology; D006801:Humans; D008213:Lymphocyte Activation; D008214:Lymphocytes / Q000032:analysis* / Q000378:metabolism; D008565:Membrane Proteins / Q000032:analysis* / Q000302:isolation & purification / Q000378:metabolism; D008970:Molecular Weight; D009124:Muscle Proteins / Q000378:metabolism; D010455:Peptides / Q000032:analysis; D010750:Phosphoproteins / Q000032:analysis* / Q000302:isolation & purification / Q000378:metabolism; D010766:Phosphorylation; D019000:Phosphotyrosine; D051381:Rats; D012697:Serine Endopeptidases / Q000378:metabolism; D014443:Tyrosine / Q000031:analogs & derivatives* / Q000032:analysis / Q000378:metabolism; D016596:Vinculin
D002147:Calmodulin; D002148:Calmodulin-Binding Proteins; D008565:Membrane Proteins; D009124:Muscle Proteins; D010455:Peptides; D010750:Phosphoproteins; D003208:Concanavalin A; D016596:Vinculin; D019000:Phosphotyrosine; D014443:Tyrosine; D012697:Serine Endopeptidases; C028344:glutamyl endopeptidase