Irreversible thiophosphorylation and activation of tension in functionally skinned rabbit ileum strips by [35S]ATP gamma S.
Irreversible thiophosphorylation and activation of tension in functionally skinned rabbit ileum strips by [35S]ATP gamma S.
复制标题
[35S]ATP gamma S 对功能性去皮兔回肠条进行不可逆硫代磷酸化和张力激活。
DOI:
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发表时间:
1979
影响因子:
4.8
通讯作者:
W. Kerrick
中科院分区:
文献类型:
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作者:
P. Cassidy;P. E. Hoar;W. Kerrick
Rabbit ileum strips were functionally skinned by exposure to staphylococcal alpha-toxin. Incubation of the strips in the ATP analog ATP gamma S or [35S]ATP gamma S in the presence of Ca2+ (but not in the absence of Ca2+) resulted in a maximal Ca2+-insensitive activated tension that persisted following removal of Ca2+. Correlated with this tension was 35S-labeling of the 20,000-dalton myosin light chain, LC20, that persisted even after removal of Ca2+. Tension in these strips partially relaxed when exposed to ATP (alpha,beta-methylene). In contrast, alpha-toxin-treated strips exposed to ATP or [gamma-32P]ATP showed Ca2+-sensitive, reversible activated tension and reversible 32P-labeling of the LC20. These results are consistent with a currently proposed model of Ca2+ control of smooth muscle contraction involving a myosin light chain kinase-phosphatase system.