descriptionPublicationkeyboard_double_arrow_right Article 01 Jan 1989 English Publisher:Elsevier BVJournal:Comparative Biochemistry and Physiology Part B: Comparative Biochemistry, volume 94, pages 813-821 (issn: 0305-0491,

Authors: David J. Hartshorne; Takahide Tsuchiya; Shugo Watabe;

doi: 10.1016/0305-0491(89)90171-5

pmid: 2532591

Phosphorylation of paramyosin

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Abstract

1. Myofibrils isolated from Mercenaria mercenaria were phosphorylated by endogenous kinase. Over a range of ionic strengths only paramyosin was phosphorylated. 2. Thiophosphorylation of paramyosin caused an inhibition of steady-state actin-activated ATPase activity of the myofibrils. 3. It is proposed that the endogenous kinase is the catalytic subunit of the cAMP-dependent protein kinase. 4. The sequence around the phosphorylation site was determined. 5. The phosphorylation site probably is close to the C-terminus of the paramyosin molecule.

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Keywords

Binding Sites, Mollusca, Animals, Ca(2+) Mg(2+)-ATPase, Tropomyosin, Myosins, Phosphorylation, Protein Kinases, Muscle Contraction

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