Ojima T, Nishita K, Watanabe S
J Biochem. 1984 Oct;96(4):1109-15. doi: 10.1093/oxfordjournals.jbchem.a134928.
It was shown in our previous report (Ojima et al. (1983) J. Biochem. 94, 307-310) that hybridization of Akazara scallop "desensitized" myosin with rabbit skeletal DTNB-light chains led to inhibition of the Mg-ATPase activity of acto-desensitized myosin but to enhancement of its superprecipitation activity. The following are now found: Development of tension in desensitized glycerinated fibers of Akazara adductor is significantly improved when DTNB-light chains are added to the fiber bath. The actin-affinity of desensitized heavy meromyosin in the presence of ATP but in the absence of Ca2+ is decreased by hybridization with chicken gizzard 20K dalton-light chains but significantly increased by that with DTNB-light chains. It is therefore suggested that the increase in actin-binding may account for the enhancing effect of DTNB-light chains on the superprecipitation and on the tension development.
我们之前的报告(小岛等人(1983年)《生物化学杂志》94卷,307 - 310页)表明,赤坂扇贝“脱敏”肌球蛋白与兔骨骼肌二硫硝基苯甲酸(DTNB)轻链杂交会抑制肌动蛋白脱敏肌球蛋白的Mg - ATP酶活性,但会增强其超沉淀活性。现在发现以下情况:当将DTNB轻链添加到纤维浴中时,赤坂闭壳肌脱敏甘油化纤维中的张力发展得到显著改善。在存在ATP但不存在Ca2 +的情况下,脱敏重酶解肌球蛋白与鸡砂囊20K道尔顿轻链杂交会降低其肌动蛋白亲和力,但与DTNB轻链杂交则会使其显著增加。因此,有人提出肌动蛋白结合的增加可能是DTNB轻链对超沉淀和张力发展产生增强作用的原因。