Phosphorylation of soluble pig epidermal proteins by endogenous calcium-activated, phospholipid-dependent protein kinase.
Endogenous calcium-activated, phospholipid-dependent protein kinase phosphorylates pig epidermal protein. Pig epidermis was homogenized and centrifuged at 30,000 X g for 30 min. The supernatant was incubated with or without calcium and phospholipid. A 97 kD soluble protein from pig epidermis was phosphorylated in the presence of calcium and phosphatidylserine. The phosphorylation reaction occurred immediately. With the use of two-dimensional polyacrylamide gel electrophoresis, it was shown that the 97 kD fragment was a basic protein, and that several small proteins were also phosphorylated. The characterization of these proteins is yet to be undertaken.
D000818:Animals; D002118:Calcium / Q000494:pharmacology; D004817:Epidermis / Q000378:metabolism*; D066298:In Vitro Techniques; D010743:Phospholipids / Q000494:pharmacology; D010766:Phosphorylation; D011493:Protein Kinase C / Q000378:metabolism*; D011506:Proteins / Q000378:metabolism*; D012995:Solubility; D013552:Swine
D010743:Phospholipids; D011506:Proteins; D011493:Protein Kinase C; D002118:Calcium