Changes in Light Scattering Intensity of Fish Holo-, Apo- and Reconstituted Myoglobins under Thermal Denaturation

Fisheries Science

Volumn 64, Issue 5, 1998, Pages 846-847

  Chanthai, Saksit ^a   Nieda, Hidekazu ^a   Ogawa, Masahiro ^a   Tamiya, Toru ^a   Tsuchiya, Takahide ^a  

^a SOPHIA UNIVERSITY   (Japan)

Author keywords

Light scattering intensity; Myoglobin; Protein stability; Thermal denaturation

Indexed keywords

EID: 0345917663     PISSN: 09199268     EISSN: None     Source Type: Journal    
DOI: 10.2331/fishsci.64.846     Document Type: Article

References (5)

1. S. Chanthai, M. Ogawa, T. Tamiya, and T. Tsuchiya: Studies on thermal denaturation of fish myoglobins using differential scanning calorimetry, circular dichroism, and tryptophan fluorescence. Fisheries Sci., 62, 927-932 (1996).
2. S. Chanthai, M. Ogawa, T. Tamiya, and T. Tsuchiya: Studies on thermal denaturation of fish apomyoglobins using differential scanning calorimetry, circular dichroism, and fluorescence. Fisheries Sci., 62, 933-937 (1996).
3. S. Chanthai, M. Ogawa, T. Tamiya, and T. Tsuchiya: Studies on thermal denaturation profiles of holo- and reconstituted myoglobins from bonito and sperm whale. Fisheries Sci., (submitted) (1997).
4. A. Rossi-Fanelli, E. Antonini, and R. Giuffre: Oxygen equilibrium of myoglobin from Thunnus thynnus. Nature, 186, 896-897 (1960).
5. K. Yamaguchi, N. Takeda, K. Ogawa, and K. Hashimoto: Properties of mackerel and sardine myoglobins. Bull. Japan. Soc. Sci. Fish., 45, 1335-1339 (1979).