Age-dependent changes in the level of a 22 KDa plasma membrane phosphoprotein in developing chick embryo brain.
In vitro phosphorylation of brain proteins of developing chick embryos showed a drastic increase in the extent of phosphorylation of a 22 KDa protein from the fourteenth day reaching a peak at seventeenth day of development; the phosphorylation of the 22 KDa protein declined afterwards. Phosphoaminoacid analysis of the 22 KDa protein indicated serine residues as targets of phosphorylation. Isoelectric focusing followed by second dimensional SDS-PAGE indicated that the 22 KDa protein had a pI value of 4.5. Polymyxin B, an inhibitor of Ca2+ and phospholipid dependent protein kinases inhibited the phosphorylation of the 22 KDa protein.
David
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E
Cancer Biology Division, School of Biological Sciences, Madurai Kamaraj University, India.
Shanmugam
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G
D000375:Aging / Q000378:metabolism*; D000818:Animals; D001921:Brain / Q000196:embryology / Q000378:metabolism*; D002462:Cell Membrane / Q000187:drug effects / Q000378:metabolism; D002642:Chick Embryo; D008565:Membrane Proteins / Q000378:metabolism; D008970:Molecular Weight; D010750:Phosphoproteins / Q000378:metabolism*; D010766:Phosphorylation; D011112:Polymyxin B / Q000494:pharmacology
D008565:Membrane Proteins; D010750:Phosphoproteins; D011112:Polymyxin B