Disulfide-linked dimer of oncomodulin: comparison to calmodulin.
Disulfide-linked dimer of oncomodulin: comparison to calmodulin.
复制标题
癌调节蛋白二硫键连接的二聚体:与钙调节蛋白的比较。
DOI:
10.1021/bi00415a033
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发表时间:
1988
期刊:
影响因子:
2.9
通讯作者:
J. Macmanus
中科院分区:
文献类型:
--
作者:
B. Mutus;E. J. Palmer;J. Macmanus
Oncomodulin, an oncofetal Ca2+-binding protein, contains a single Cys residue in position 18 of its primary structure. The reactivity of the Cys-18 thiol has been probed with 5,5'-dithiobis(2-nitrobenzoate) (NbS2). The kinetics of the reaction indicate that the thiol group is approximately 10-fold more reactive in the presence of Ca2+ than in its absence. Evidence presented here shows that oncomodulin can dimerize by intermolecular disulfide formation via the Cys-18 thiol. The kinetics of dimer formation indicate that the second-order rate constant for this reaction is approximately 6-fold higher than that observed for the reaction of the Cys-18 thiol with NbS2, possibly indicating that intermolecular electrostatic interactions precede disulfide formation. The disulfide-linked dimer of oncomodulin appears to be more similar to calmodulin than oncomodulin since the dimer displayed "calmodulin-like" affinity for the amphiphilic peptide melittin. In addition, oncomodulin dimer was shown to activate two calmodulin-dependent enzymes, cyclic nucleotide phosphodiesterase and calcineurin phosphatase, with the activity constants of 63 and 1 nM, respectively, indicating that these enzymes have different domain contact requirements for activation.
DOI:
--
发表时间:
1986
期刊:
The Journal of biological chemistry
影响因子:
--
作者:
Putkey,JA;Draetta,GF;Slaughter,GR;Klee,CB;Cohen,P;Stull,JT;Means,AR
通讯作者:
Means,AR
DOI:
--
发表时间:
1986
期刊:
The Journal of biological chemistry
影响因子:
--
作者:
Hansen,RS;Beavo,JA
通讯作者:
Beavo,JA
影响因子:
2.9
作者:
MALENCIK, DA;ANDERSON, SR
通讯作者:
ANDERSON, SR