title: Structural stability of fish myosin subfragment-1.
abstract: 1. Tryptic cleavage of fish myosin subfragment-1 (S-1) revealed its similar substructure of heavy chain to that of rabbit S-1. 2. The structural stability of fish S-1 was studied by thermal denaturation method, and a rapid polymerization of inactivated fish S-1, detected by turbidity increase, was characteristic. 3. The light-chain release and tryptic susceptibility increase upon heating were significant with fish S-1.
authors.affiliation: Department of Food Science, Faculty of Fisheries, Hokkaido University, Japan.
authors.forename: M
authors.initials: M
authors.lastname: Hamai
authors.forename: K
authors.initials: K
authors.lastname: Konno
mesh_terms: D000818:Animals; D002347:Carps / Q000378:metabolism*; D002850:Chromatography, Gel; D003530:Cyprinidae / Q000378:metabolism*; D006358:Hot Temperature; D015879:Myosin Subfragments; D009391:Nephelometry and Turbidimetry; D011489:Protein Denaturation; D011817:Rabbits; D012685:Sepharose / Q000031:analogs & derivatives; D013045:Species Specificity; D014357:Trypsin
chemical_list: D015879:Myosin Subfragments; C035771:Sepharose CL 4B; D012685:Sepharose; D014357:Trypsin