![]() LYS-LYS-ARG-ALA-ALA-ARG-ALA-THR-SER-NH2结构式
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常用名 | LYS-LYS-ARG-ALA-ALA-ARG-ALA-THR-SER-NH2 | 英文名 | LYS-LYS-ARG-ALA-ALA-ARG-ALA-THR-SER-NH2 |
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CAS号 | 119386-39-9 | 分子量 | 987.16100 | |
密度 | N/A | 沸点 | N/A | |
分子式 | C40H78N18O11 | 熔点 | N/A | |
MSDS | 中文版 美版 | 闪点 | N/A |
Minimum requirements for inhibition of smooth-muscle myosin light-chain kinase by synthetic peptides.
Biochem. J. 257 , 73, (1989) Although the amino acid residues that are important for peptide substrates of myosin light-chain kinase have been reported, those that are important for peptide inhibitors of this enzyme have not previously been investigated. Synthetic peptides based on the s... |
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Smooth muscle myosin kinase requires residues on the COOH-terminal side of the phosphorylation site. Peptide inhibitors.
J. Biol. Chem. 261 , 25, (1986) The COOH-terminal residue in peptide analogs of the phosphorylation site sequence in smooth muscle myosin light chains, Lys11-Lys12-Arg13-Ala-Ala-Arg16-Ala-Thr-Ser19 -(P)Asn20-Val21-Phe22-Ala23, were shown to have a strong influence on the kinetics of peptide... |
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Rabbit skeletal muscle myosin light chain kinase. The calmodulin binding domain as a potential active site-directed inhibitory domain.
J. Biol. Chem. 262 , 11958-11963, (1987) A synthetic peptide modeled after the calmodulin (CaM)-binding domain of rabbit skeletal muscle myosin light chain kinase, Lys-Arg-Arg-Trp-Lys5-Lys-Asn-Phe-Ile-Ala10-Val-Ser-Ala-Ala-+ ++Asn15-Arg-Phe-Glycyl amide (M5), inhibited the CaM-independent chymotrypt... |
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