Chicken gizzard: relation between calcium-activated phosphorylation and contraction
Of the proteins in mechanically disrupted chicken gizzard fibers (no functional sarcolemma) only the 20,000-dalton light chains of myosin underwent large Ca$^{2+}$-and Sr$^{2+}$-dependent changes in phosphorylation. Phosphorylation closely corresponded with the Ca$^{2+}$- and Sr$^{2+}$-activated ten...
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Veröffentlicht in: | Science (American Association for the Advancement of Science) 1979-05, Vol.204 (4392), p.503-506 |
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Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | Of the proteins in mechanically disrupted chicken gizzard fibers (no functional sarcolemma) only the 20,000-dalton light chains of myosin underwent large Ca$^{2+}$-and Sr$^{2+}$-dependent changes in phosphorylation. Phosphorylation closely corresponded with the Ca$^{2+}$- and Sr$^{2+}$-activated tensions. Adenosine 5′-O (3′-thiotriphosphate) only in the presence of Ca$^{2+}$ induced irreversible Ca$^{2+}$-insensitive activation of tension and thiophosphorylation of the 20,000-dalton light chains, and blocked incorporation of $^{32}$P from [γ-$^{32}$P]adenosine triphosphate into the myosin light chains. |
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ISSN: | 0036-8075 1095-9203 |
DOI: | 10.1126/science.432654 |