Turkey gizzard caldesmon molecular weight and shape.

Turkey gizzard caldesmon molecular weight and shape.
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火鸡砂囊卡尔德蒙的分子量和形状。

DOI:
10.1006/abbi.1994.1356
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发表时间:
1994
影响因子:
3.9
通讯作者:
Graceffa,P
Graceffa,P
中科院分区:
生物学3区
文献类型:
--
作者:
Stafford,WF;Chalovich,JM;Graceffa,P

文献摘要

被引文献

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用超速离心沉淀法测得鸡肌钙蛋白的相对分子质量为93±4 kDa[P.Graceffa,C.-L.A.Wang,W.F.Stafford(1988)J.Biol]。化学263,14196-14202]。另一个小组用同样的技术测定了火鸡肌胃的分子量为75±2 kDa[D.A.Malecik,J.Ausio,C.E.Byles,B.modrell,and S.R.Anderson(1989)BioChemical 28,8227-8233]。通过沉降平衡分析对火鸡蛋白的相对分子质量进行了重新估算,测得其相对分子质量为90±3 kDa,表明火鸡的肌钙蛋白是一种典型的肌钙蛋白,不属于较小的非肌钙蛋白。在十二烷基硫酸钠存在下的聚丙烯酰胺凝胶电泳法中,这两个肌钙蛋白没有合并,表明它们具有不同的氨基酸序列。
The molecular weight of chicken gizzard muscle caldesmon has been measured previously by sedimentation equilibrium in the analytical ultracentrifuge and found to be 93 ± 4 kDa [P. Graceffa, C.-L. A. Wang, and W. F. Stafford (1988)J. Biol. Chem.263, 14196-14202]. The molecular weight of turkey gizzard caldesmon has been determined by another group to be 75 ± 2 kDa by the same technique [D. A. Malecik, J. Ausio, C. E. Byles, B. Modrell, and S. R. Anderson (1989)Biochemistry28, 8227-8233]. We have reevaluated the molecular weight of the turkey protein by sedimentation equilibrium analysis and found a value of 90 ± 3 kDa, indicating that turkey gizzard caldesmon is a typical muscle caldesmon and does not belong to the class of smaller nonmuscle caldesmons. The two muscle caldesmons do not comigrate during polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate, indicating that they have different amino acid sequences.