醛缩酶与骨骼肌含肌动蛋白丝结合时动力学参数的改变。
Modification of the kinetic parameters of aldolase on binding to the actin-containing filaments of skeletal muscle.
作者信息
Walsh T P, Clarke F M, Masters C J
出版信息
Biochem J. 1977 Jul 1;165(1):165-7. doi: 10.1042/bj1650165.
Abstract
The kinetic parameters of fructose bisphosphate aldolase (EC 4.1.2.13) were shown to be modified on binding of the enzyme to the actin-containing filaments of skeletal muscle. Although binding to F-actin or F-actin-tropomyosin filaments results in relative minor changes in kinetic properties, binding to F-actin-tropomyosin-troponin filaments produces major alterations in the kinetic parameters, and, in addition, renders them Ca2+-sensitive. These observations may be relevant to an understanding of the function of this enzyme within the muscle fibre.
摘要
已表明，果糖二磷酸醛缩酶（EC 4.1.2.13）的动力学参数在该酶与骨骼肌含肌动蛋白的细丝结合时会发生改变。尽管与F-肌动蛋白或F-肌动蛋白-原肌球蛋白细丝结合会导致动力学性质发生相对较小的变化，但与F-肌动蛋白-原肌球蛋白-肌钙蛋白细丝结合会使动力学参数发生重大改变，此外，还使其对Ca2+敏感。这些观察结果可能有助于理解该酶在肌纤维中的功能。
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