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Phosphorylation by protein kinase C of a synthetic heptapeptide bearing a lysine residue on the C terminal side of serine
Authors:H Kondo  Y Baba  K Takaki  K Kondo  H Kagamiyama
Affiliation:1. Laboratory of Bioorganic Chemistry, Department of Industrial Chemistry, Nagasaki University, Nagasaki 852, Japan;2. Department of Medical Chemistry, Osaka Medical College, Takatsuki, Osaka 569, Japan;1. Department of Oncology, The First Affiliated Hospital of Anhui Medical University, Hefei, 230002, China;2. Anhui Public Health Clinical Center, Hefei, 230002, China;1. State Key Laboratory of Biotherapy, West China Hospital, Sichuan University, Chengdu, Sichuan, China;2. Thoracic Oncology Ward, Cancer Center, and State Key Laboratory of Biotherapy, West China Hospital, Sichuan University, Chengdu, Sichuan, China;3. NHC Key Laboratory of Nuclear Technology Medical Transformation, Mianyang Central Hospital, School of Medicine, University of Electronic Science and Technology of China, Mianyang, Sichuan, China;1. Zhongda Hospital, Medical School, Advanced Institute for Life and Health, Southeast University, Nanjing, 210096, China;2. Shanxi Academy of Advanced Research and Innovation, Taiyuan, 030032, China;3. Zhongda Hospital, School of Life Sciences and Technology, Advanced Institute for Life and Health, Southeast University, Nanjing, 210096, China;4. The People''s Hospital of Guizhou Province, Guiyang, 550002, China;5. Nanjing University Medical School, Nanjing, 210046, China
Abstract:A peptide, Ala-Ser-Gly-Ser-Phe-Lys-Leu, which corresponds to Ala103-Leu109 of Hl histone, was synthesized and tested as substrate for protein kinase C. The serine residue at position 4 was phosphorylated specifically. Another peptide lacking the lysine at position 6 was not phosphorylated by the same enzyme, indicating the importance of that basic residue as the recognition site for protein kinase C.
Keywords:
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