Two highly homologous synthetic peptides MLC(3-13) (K-R-A-K-A-K-T-TK-K-R-G) and MLC(5-13) (A-K-A-K-T-T-K-K-R-G) corresponding to the amino terminal amino acid sequence of smooth muscle myosin light chain were utilized as substrates for protein kinase C purified from murine lymphosarcoma tumors to determine the role of the primary amino acid sequence of protein kinase C substrates in defining the lipid (phosphatidyl serine and diacylglycerol) requirements for the activation of the enzyme. Removal of the basic residues lysine and arginine from the amino terminus of MLC(3-13) did not have a significant effect on the Ka value of diacylglycerol. The binding of effector to calcium-protein kinase C appears to be random since binding of one effector did not block the binding of the other.
| Identifer | oai:union.ndltd.org:unt.edu/info:ark/67531/metadc277577 |
| Date | 08 1900 |
| Creators | Abukhalaf, Imad Kazem |
| Contributors | Masaracchia, Ruthann A., Wu, Edward Ming-chi, 1938-, Easom, Richard, Donahue, Manus J., Norton, S. J., Shanley, Mark Stephen |
| Publisher | University of North Texas |
| Source Sets | University of North Texas |
| Language | English |
| Detected Language | English |
| Type | Thesis or Dissertation |
| Format | xii, 151 leaves : ill., Text |
| Rights | Public, Copyright, Copyright is held by the author, unless otherwise noted. All rights reserved., Abukhalaf, Imad Kazem |
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