skip to main content
OSTI.GOV title logo U.S. Department of Energy
Office of Scientific and Technical Information

Title: Differential phosphorylation of multiple sites in protein 4. 1 and protein 4. 9 by phorbol ester-activated and cyclic AMP-dependent protein kinases

Journal Article · · J. Biol. Chem.; (United States)
OSTI ID:6335772

The phosphorylation of the membrane skeleton components protein 4.1 and protein 4.9 in intact erythrocytes is shown to increase in the presence of either 1 microM 12-O-tetradecanoyl phorbol 13-acetate or 2 mM dibutyryl cAMP. The phosphorylation induced by these protein kinase activators is compared by two-dimensional tryptic peptide mapping. In both proteins, the pattern of peptides phosphorylated in the presence of 12-O-tetradecanoyl phorbol 13-acetate differs from the pattern of peptides phosphorylated in the presence of dibutyryl cAMP. The relative locations of the phosphorylated sites on protein 4.1 have been determined using limited proteolysis by alpha-chymotrypsin.

Research Organization:
Yale Univ. School of Medicine, New Haven, CT
OSTI ID:
6335772
Journal Information:
J. Biol. Chem.; (United States), Vol. 16
Country of Publication:
United States
Language:
English