Bárány M, Rokolya A, Bárány K
Department of Biochemistry, College of Medicine, University of Illinois Chicago 60612.
FEBS Lett. 1991 Feb 11;279(1):65-8. doi: 10.1016/0014-5793(91)80252-x.
We have tested the hypothesis of Winder and Walsh [(1990) J. Biol. Chem. 265, 10148] that the contractile state of smooth muscle is regulated by calponin phosphorylation. Porcine carotid arterial muscles were highly labeled with 32P, then contracted with four different agents for various times. No radioactivity was detected in calponin isolated by 2D or 1D gel electrophoresis from the muscles. Similarly, resting muscles showed no [32P]phosphate in calponin. Apparently the sites of calponin available for phosphorylation in vitro are rendered unavailable in the intact muscle.
我们检验了温德(Winder)和沃尔什(Walsh)提出的假设[(1990年)《生物化学杂志》265卷,第10148页],即平滑肌的收缩状态受钙调蛋白磷酸化调节。用³²P对猪颈动脉肌肉进行高度标记,然后用四种不同的试剂使其收缩不同时间。通过二维或一维凝胶电泳从肌肉中分离出的钙调蛋白未检测到放射性。同样,静息肌肉的钙调蛋白中也没有[³²P]磷酸盐。显然,在完整肌肉中,体外可用于磷酸化的钙调蛋白位点变得不可用。