In situ phosphorylation of contractile proteins of a molluscan Mytilus edulis catch muscle in different functional states |
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| Affiliation: | 1. Department of Animal Science, Michigan State University, East Lansing, MI, 48824, USA;2. Animal Science and Food Science and Human Nutrition, Michigan State University, East Lansing, MI, 48824, USA;1. Human Performance Laboratory, Faculty of Kinesiology, University of Calgary, Calgary, Canada;2. FH JOANNEUM, Department of Engineering, University of Applied Science, Graz, Austria;1. School of Physical Therapy and Graduate Institute of Rehabilitation Science, College of Medicine, Chang Gung University, Taoyuan, Taiwan;2. Chang Gung Memorial Hospital, Neuroscience Research Center, Linkou, Taoyuan, Taiwan;3. Department of Physical Therapy and Rehabilitation Science, Roy and Lucille Carver College of Medicine, The University of Iowa, Medical Education Building, Iowa City, IA, USA;4. Department of Internal Medicine, Roy and Lucille Carver College of Medicine, The University of Iowa, Iowa City, IA, USA |
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| Abstract: | - 1.1. The incorporation of 32P into the contractile proteins of the anterior byssus retractor muscle of Mytilus edilus L. was analyzed during the different stages of a contraction-catch-relaxatin cycle.
- 2.2. The experiments were performed with saponin-skinned fibers preincubated with γ-32P-ATP.
- 3.3. The total amount of 32P incorporated into the fiber proteins was anlyzed by measuring the label of TCA-insoluble protein in a scintillation counter.
- 4.4. The dose incorporated was about twice as high during Ca2+ induced contraction and serotonin induced accelerated relaxation as during test and catch.
- 5.5. The molecular mass of the phosphorylated proteins was analyzed by autoradiography of the proteins separated by SDS-PAGE.
- 6.6. Up to 26 protein spots of different molecular masses were labelled, including such well characterized protein spe+cies as myosin heavy and light chains, paramyosin and tropomyosin.
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