Hoar P E, Kerrick W G, Cassidy P S
Science. 1979 May 4;204(4392):503-6. doi: 10.1126/science.432654.
Of the proteins in mechanically disrupted chicken gizzard fibers (no functional sarcolemma) only the 20,000-dalton light chains of myosin underwent large Ca2+-and Sr2+-dependent changes in phosphorylation. Phosphorylation closely corresponded with the Ca2+- and Sr2+-activated tensions. Adenosine 5'-O (3'-thiotriphosphate) only in the presence of Ca2+ induced irreversible Ca2+-insensitive activation of tension and thiophosphorylation of the 20,000-dalton light chains, and blocked incorporation of 32P from [gamma-32P]adenosine triphosphate into the myosin light chains.
在机械破碎的鸡胗纤维（无功能性肌膜）中的蛋白质中，只有肌球蛋白的20,000道尔顿轻链发生了依赖于Ca2+和Sr2+的大量磷酸化变化。磷酸化与Ca2+和Sr2+激活的张力密切相关。5'-O（3'-硫代三磷酸）腺苷仅在Ca2+存在时诱导不可逆的Ca2+不敏感的张力激活和20,000道尔顿轻链的硫代磷酸化，并阻止[γ-32P]三磷酸腺苷中的32P掺入肌球蛋白轻链。
