Caldesmon, a calmodulin‐binding, F actin‐interacting protein, is present in aorta, uterus and platelets

FEBS Letters

Kakiuchi, Ritsu¹  Sobue, Kenji¹  Kanda, Keiko¹  Morimoto, Kouichi¹  Inui, Makoto¹  Kakiuchi, Shiro¹ 

[1] Department of Neurochemistry and Neuropharmacology, Institute of Higher Nervous Activity, Osaka University Medical School, Nakanoshima, Kita-ku, Osaka 530, Japan

关键词: Calmodulin;    Calmodulin-binding protein;    Actin binding;    Smooth muscle contraction;    Platelet contractile protein;    Flip-flop mechanism;    EGTA;    ethylene glycol bis(β-aminoethyl ether)-N;    N;    N′;    N′-tetraacetic acid;    SDS;    sodium dodecyl sulfate;    PBS;    phosphate-buffered saline (20 mM sodium phosphate buffer;    pH 7.4;    and 150 mM NaCl);   

DOI  :  10.1016/0014-5793(83)80181-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Caldesmon, a protein originally found in chicken gizzard, was concluded also to be present in bovine aorta, uterus, and human platelets by demonstration of a protein with the following properties: (a) Ca²⁺-dependent calmodulin-binding; (b) binding to F actin in such way that the binding was broken on Ca²⁺-dependent binding of calmodulin; (c) cross-reactivity in immune blotting procedures with affinity-purified antibody against gizzard caldesmon; (d) similar subunit M _r-values on SDS-gel to those of gizzard caldesmon. Like gizzard caldesmon, platelet caldesmon was composed of two polypeptide bands of M _r 150000 and 147000, but caldesmon in aorta and uterus gave a single band of M _r 150000. A polypeptide of M _r 165000 that was immunologically distinct from caldesmon but, like caldesmon, bound to calmodulin and F actin in a flip-flop fashion, was also demonstrated in aorta and uterus.

【 授权许可】

Unknown