Comparison of the stability of fish light meromyosins by guanidine hydrochloride denaturation

Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology

Volumn 122, Issue 4, 1999, Pages 439-446

  Ogawa, Masahiro ^a,b   Miyagi, Ryoko ^a   Tamiya, Toru ^a   Tsuchiya, Takahide ^a  

^a SOPHIA UNIVERSITY   (Japan)

^b UNIVERSITY OF BRITISH COLUMBIA   (Canada)

Author keywords

Circular dichroism; Fish; Fluorescence; Guanidine hydrochloride; Light meromyosin; Myosin rod; Tryptophan; Helix

Indexed keywords

GUANIDINE; MYOSIN; MYOSIN LIGHT CHAIN; TRYPTOPHAN;

ALPHA HELIX; ANIMAL TISSUE; ARTICLE; BODY TEMPERATURE; CARP; CIRCULAR DICHROISM; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; DENATURATION; FISH; FLUORESCENCE; FLUORESCENCE SPECTROSCOPY; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN STABILITY; RABBIT; WATER TEMPERATURE;

CYPRINUS CARPIO; ORYCTOLAGUS CUNICULUS;

EID: 0032930419     PISSN: 03050491     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0305-0491(99)00023-1     Document Type: Article

References (33)

1. Ahmad F, Bigelow CC. Estimation of the free energy of stabilization of ribonuclease A, lysozyme, α-lactalbumin, and myoglobin. J Biol Chem 1982;257:12935-8.
2. Arai K, Kawamura K, Hayashi C. The relative thermostabilities of the actomyosin - ATPase from the dorsal muscles of various fish species. Nippon Suisan Gakkaishi 1973;39:1077-85.
3. Aune KC, Tanford C. Thermodynamics of the denaturation of lysozyme by guanidine hydrochloride. II. Dependence on denaturant concentration at 25°. Biochemistry 1969;8:4586-90.
4. Barrick D, Baldwin RL. Three-state analysis of sperm whale apomyoglobin folding. Biochemistry 1993;32:3790-6.
5. Bertazzon A, Tsong TY. Effects of ions and pH on the thermal stability of thin and thick filaments of skeletal muscle: high-sensitivity differential scanning calorimetric study. Biochemistry 1990;29:6453-9.
6. Burke M, Himmelfarb S, Harrington WF. Studies on the 'Hinge' region of myosin. Biochemistry 1973;12:701-10.
7. Connell JJ. The relative stabilities of the skeletal muscle myosins of some animals. Biochem J 1961;80:503-9.
8. Green RF Jr., Pace CN. Urea and guanidine hydrochloride denaturation of ribonuclease, lysozyme, α-chymotrypsin, and β-lactoglobulin. J Biol Chem 1974;249:5388-93.
9. Johnston IA, Frearson N, Goldspink G. The effects of environmental temperature on the properties of myofibrillar adenosine triphosphatase from various species of fish. Biochem J 1973;133:735-8.
10. Kato S, Konno K. Isolation of carp myosin rod and its structural stability. Nippon Suisan Gakkaishi 1993;59:539-44.
11. King L, Lehrer SS. Thermal unfolding of myosin rod and light meromyosin: circular dichroism and tryptophan fluorescence studies. Biochemistry 1989;28:3498-502.
12. Laemmli UK Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970;227:680-5.
13. Maeda K, Sczakiel G, Wittinghofer A. Characterization of cDNA coding for the complete light meromyosin portion of a rabbit fast skeletal muscle myosin heavy chain. Eur J Biochem 1987;167:97-102.
14. Maita T, Yajima E, Nagata S, Miyanishi T, Nakayama S, Matsuda G. The primary structure of skeletal muscle myosin heavy chain: IV. sequence of the rod, and the complete 1938-residue sequence of the heavy chain. J Biochem (Tokyo) 1991;110:75-87.
15. Margossian SS, Lowey S. Preparation of myosin and its subfragments from rabbit skeletal muscle. In: Frederiksen DW, Cunningham LW, editors. Methods in Enzymolology, vol. 85. New York: Academic Press, 1982:55-71.
16. Matthews CR, Crisanti MM. Urea-induced unfolding of the α subunit of tryptophan synthesis: evidence for a multistate process. Biochemistry 1981;20:784-92.
17. Nakaya M, Watabe S, Ooi T. Differences in the thermal stability of acclimation temperature-associated type of carp myosin and its rod on differential scanning calorimetry. Biochemistry 1995;34:3114-20.
18. Nitta T, Itazawa Y. Fish. In: Nitta T, Itazawa Y, editors. Suisan Seibutsu Tekisuionzu. Tokyo: Japan Fisheries Resource Conservation Association, 1980:7-29 (in Japanese).
19. Nyitray L, Goodwin EB, Szent-Györgyi AG. Complete primary structure of a scallop striated muscle myosin heavy chain. J Biol Chem 1991;266:18469-76.
20. Ogawa M, Tamiya T, Tsuchiya T. Structural changes of carp myosin during heating. Fish Sci 1994;60:723-7.
21. Ogawa M, Tamiya T, Tsuchiya T. Thermal stability of α-helical structure of fish myosin rods. Comp Biochem Physiol 1995;110B:367-70.
22. Pace CN. Determination and analysis of urea and guanidine hydrochloride denaturation curves. In: Hirs CHW, Timasheff SN, editors. Methods in Enzymology, vol. 131. New York: Academic Press, 1986:266-80.
23. Pace CN, Vanderburg KE. Determining globular protein stability: guanidine hydrochloride denaturation of myoglobin. Biochemistry 1979;18:288-92.
24. Perry SV. Myosin adenosinetriphosphatase. In: Colowick SP, Kaplan NO, editors. Methods in Enzymology, vol. 2. New York: Academic Press, 1955:582-8.
25. Potekhin SA, Trapkov VA, Privalov PL. Stepwise pattern of the thermal denaturing of helical fragments of myosin. Biophysics 1979;24:45-50.
26. Rodgers ME, Karr T, Biedermann K, Ueno H, Harrington WF. Thermal stability of myosin rod from various species. Biochemistry 1987;26:8703-8.
27. Saez L, Leinwand LA. Characterization of diverse forms of myosin heavy chain expressed in adult human skeletal muscle. Nucleic Acids Res 1986;14:2951-69.
28. Sohn RL, Vikstrom KL, Strauss M, Cohen C, Szent-Gyorgyi AG, Leinwand LA. A 29 residue region of the sarcomeric myosin rod is necessary for filament formation. J Mol Biol 1997;266:317-30.
29. Tanford C. Protein denaturation. In: Anfinsen CBJR, Edsall JT, Richards FM, editors. Advances in Protein Chemistry, vol. 24. New York: Academic Press, 1975:1-95.
30. Tsuchiya T, Matsumoto JJ. Isolation, purification and structure of carp myosin, HMM and LMM. Nippon Suisan Gakkaishi 1975;41:1319-26.
31. Umemoto S. A modified method for estimation of fish muscle protein by the biuret method. Nippon Suisan Gakkaishi 1966;32:427-35 (in Japanese).
32. Watabe S. GenBank accession numbers D89990; D89991; D89992; 1997.
33. Watabe S, Imai J, Nakaya M, Hirayame Y, Okamoto Y, Masaki H, Uozumi T, Hirono I, Aoki T. Temperature acclimation induced light meromyosin isoforms with different primary structures in carp fast skeletal muscle. Biochem Biophys Res Commun 1995;208:118-25.