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Characterization and partial purification of a high-molecular-mass, calmodulin-binding, tyrosyl-phosphorylated
1Max Planck Institut für Biochemie, Martinsried, Federal Republic of Germany.
Experimental Cell Research
|March 1, 1989
Abstract:
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.