Complete nucleotide sequences of cDNA encoding for tropomyosin isoforms from the catch muscle of scallop Patinopecten yessoensis

Hasegawa, Yasushi

doi:10.1046/j.1444-2906.2001.00352.x

Fisheries Sci

2001

DOI: 10.1046/j.1444-2906.2001.00352.x

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Complete nucleotide sequences of cDNA encoding for tropomyosin isoforms from the catch muscle of scallop Patinopecten yessoensis

Yasushi Hasegawa

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Cited by 7 publications

References 12 publications

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Biochemical and physicochemical characteristics of the major muscle proteins from fish and shellfish

Ochiai

Ozawa

2020

Fish Sci

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Fish and marine invertebrates constitute an important part of the human diet worldwide, and their muscles are the major edible parts. The muscles are a rich source of proteins, which in other terms determines the nutritional value and the quality of seafood products. Though the fish skeletal muscle proteins share many similarities with their mammalian counterparts, there exist great differences in their biological activity and structural stability. While the muscles of shellfish or aquatic invertebrates share many properties and general structural features with their vertebrate counterparts, they have unique characteristics. Therefore, understanding the biochemical and physicochemical properties of their major protein components is needed from the viewpoint of effective utilization of aquatic bioresources. Thus, in this review, we aimed to assemble the basis of such differences and also to understand the benefits of these proteins as the targets for studies on the structure–stability relationship of proteins.

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Biochemical and physicochemical characteristics of the major muscle proteins from fish and shellfish

Ochiai

Ozawa

2020

Fish Sci

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Thermodynamic characterization of muscle tropomyosins from marine invertebrates

Ozawa¹,

Watabe²,

Ochiai³

2011

Comparative Biochemistry and Physiology Part B: Biochemistry an

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Thermostability of striated and smooth adductor muscle tropomyosins from Yesso scallop Mizuhopecten yessoensis

Ozawa

Watabe

Ochiai

2010

Journal of Biochemistry

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The striated and smooth adductor muscle tropomyosins (TMs) of Yesso scallop Mizuhopecten yessoensis have been known to express different isoforms, but have not been characterized in detail to date. In the present study, TMs from both muscles of Yesso scallop were purified and their stabilities were compared by circular dichroism (CD) spectrometry and differential scanning calorimetry (DSC). From the CD data, the apparent melting temperature and the apparent free energy of folding at 20 degrees C were calculated to be 30.5 degrees C and -13.4 kJ/mol, and 36.0 degrees C and -31.9 kJ/mol for the striated and smooth muscle TMs, respectively. From the DSC data, DeltaH values were calculated to be 1.87 x 10(3) and 2.19 x 10(3) kJ/mol for striated and smooth muscle TMs. These results suggest that smooth muscle TM has higher thermostability than striated muscle TM. The amino acid residues responsible for such stability difference were considered to be the six amino acid substitutions in the middle region of the TM molecules.

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Complete nucleotide sequences of cDNA encoding for tropomyosin isoforms from the catch muscle of scallop Patinopecten yessoensis

Cited by 7 publications

References 12 publications

Biochemical and physicochemical characteristics of the major muscle proteins from fish and shellfish

Biochemical and physicochemical characteristics of the major muscle proteins from fish and shellfish

Thermodynamic characterization of muscle tropomyosins from marine invertebrates

Thermostability of striated and smooth adductor muscle tropomyosins from Yesso scallop Mizuhopecten yessoensis

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