Application of Synthetic Peptides as Substrates for Reversible Phosphorylation

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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 ... continued below

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xii, 151 leaves : ill.

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Abukhalaf, Imad Kazem August 1992.

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  • Abukhalaf, Imad Kazem

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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.

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xii, 151 leaves : ill.

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  • August 1992

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  • March 24, 2014, 8:07 p.m.

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  • Oct. 10, 2014, 8:57 a.m.

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Abukhalaf, Imad Kazem. Application of Synthetic Peptides as Substrates for Reversible Phosphorylation, dissertation, August 1992; Denton, Texas. (digital.library.unt.edu/ark:/67531/metadc277577/: accessed December 18, 2017), University of North Texas Libraries, Digital Library, digital.library.unt.edu; .