Kealey T, Randle P J
Biochem J. 1984 May 15;220(1):291-9. doi: 10.1042/bj2200291.
Actomyosin was partially purified from rat parotid cells dispersed by collagenase digestion and found to possess different solubility characteristics from that from (undispersed) rat parotid tissue. This is attributed to the decrease in vascular contamination effected by the isolation of parotid cells, yielding a non-muscle actomyosin [Adelstein, Conti, Johnson, Pastan & Pollard (1972) Proc. Natl. Acad. Sci. U.S.A. 69, 3693-3697]. Myosin light-chain kinase was partially purified from dispersed rat parotid cells by calmodulin affinity chromatography and shown to be activated by Ca2+-calmodulin. The calmodulin content of dispersed rat parotid cells was shown to be 6.50 +/- 0.59 ng of calmodulin/micrograms of rat parotid-cell protein (mean +/- S.E.M.), as determined by the activation of purified bovine brain phosphodiesterase by heat-treated extracts of dispersed rat parotid cells.
通过胶原酶消化分散大鼠腮腺细胞,从中部分纯化出肌动球蛋白,发现其溶解性特征与(未分散的)大鼠腮腺组织中的肌动球蛋白不同。这归因于腮腺细胞分离导致血管污染减少,从而产生一种非肌肉肌动球蛋白[阿德尔斯坦、孔蒂、约翰逊、帕斯坦和波拉德(1972年)《美国国家科学院院刊》69, 3693 - 3697]。通过钙调蛋白亲和层析从分散的大鼠腮腺细胞中部分纯化出肌球蛋白轻链激酶,并证明其被Ca²⁺ - 钙调蛋白激活。通过用分散的大鼠腮腺细胞热处理提取物激活纯化的牛脑磷酸二酯酶,测定出分散的大鼠腮腺细胞中钙调蛋白含量为6.50 ± 0.59纳克钙调蛋白/微克大鼠腮腺细胞蛋白(平均值 ± 标准误)。