Isolation and characterization of a calcium-binding protein derived from mRNA termed p9Ka, pEL-98, 18A2, or 42A by the newly synthesized vasorelaxant W-66 affinity chromatography.
作者： Yasuo Watanabe , Ryoji Kobayashi , Tomohiko Ishikawa , Hiroyoshi Hidaka
DOI: 10.1016/0003-9861(92)90031-Q
关键词: Biochemistry 、 Myosin light-chain kinase 、 Enzyme 、 Affinity chromatography 、 Binding protein 、 Peptide sequence 、 Chemistry 、 Calmodulin 、 Calcium-binding protein 、 Molecular mass
摘要: W-66 (N-(2-aminoethyl)-N-[2-(4-chlorocinnamylamino) ethyl]-5-isoquinolinesulfonamide), a newly synthesized isoquinolinesulfonamide, was shown to have potent vasodilatory action and calmodulin (CaM)-antagonizing action. Using the affinity chromatographic technique, we purified two Ca2+-binding proteins from EGTA-soluble fraction of bovine aorta. One CaM other an acidic protein with molecular mass 11 kDa. It tentatively named “calvasculin”. Calvasculin dimeric protein. Equilibrium dialysis showed that 1 mol calvasculin (dimer) bound 1.98 ± 0.30 Ca2+ in presence 10−3m Ca2+. failed activate Ca2+CaM-dependent enzymes such as myosin light chain kinase, phosphodiesterase, or kinase II inhibit stimulation these enzymes. The partial amino acid sequence revealed high homology predicted derived mRNA, pEL-98, 18A2, 42A, p9Ka. We also examined physicochemical biochemical properties calvasculin. antibody specific for calvasculin, obtained evidence is present abundance aorta but not brain, lung, heart, testis.
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