Phosphorylation of Membrane Proteins by Protein Kinase in a Smooth Muscle Plasma Membrane Fraction
| Autor: | Krall Jf, Stanley G. Korenman |
|---|---|
| Rok vydání: | 1982 |
| Předmět: |
Vesicle-associated membrane protein 8
Octoxynol Biology General Biochemistry Genetics and Molecular Biology Polyethylene Glycols Sarcolemma Cyclic AMP Animals Trypsin Phosphorylation Lipid bilayer Protein kinase A Cyclic GMP Integral membrane protein Cell Membrane Uterus Peripheral membrane protein Membrane Proteins Rats Inbred Strains Phosphoproteins Rats Membrane Biochemistry Membrane protein Myometrium Biophysics Female Protein Kinases cGMP-dependent protein kinase |
| Zdroj: | Experimental Biology and Medicine. 170:245-250 |
| ISSN: | 1535-3699 1535-3702 |
| DOI: | 10.3181/00379727-170-41426 |
| Popis: | Properties of protein kinase and its phosphoprotein substrates associated with a plasma membrane (sarcolemmal) fraction isolated from rat uterine smooth muscle were investigated. The enzyme, a mixture of cAMP-dependent and -independent types, was active against exogenous substrates only in the presence of Triton X-100. In contrast, a few membrane proteins were actively phosphorylated in the absence of detergent. Protein kinase was resistant to trypsin digestion when associated with the plasma membrane but not when solubilized with Triton X-100. Membrane phosphoproteins, on the other hand, were sensitive to proteolysis in their native state. These results suggest the smooth muscle sarcolemmal protein kinase interacts extensively with the membrane lipid bilayer and its intrinsic substrates, though heterogeneous, share a common membrane orientation. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|