Abstract
The hydrated volumes, Vh, of collagens extracted from various fish species were calculated by using the Simha-Einstein equation, and it was found that the hydration of warm-water fish collagen is greater than that of cold-water fish collagen (halibut). Although the intrinsic viscosities of warm-water fish (bigeye-tuna, carp and catfish) collagens are almost the same, the hydrated volume of bigeye-tuna collagen is approx. 1.5 and 3 times those of carp and catfish collagens respectively. The extent of hydration at 20 degrees C is in the following order: bigeye tuna greater than carp greater than catfish greater than halibut. The various thermodynamic activation parameters (delta G*, delta H* and delta S*) were calculated and it was found that they are useful for determining the exact denaturation temperature. It was calculated that the denaturation temperatures of halibut, bigeye-tuna, carp and catfish collagens are 17, 31, 32 and 26-30 degrees C respectively. The variations of hydration, intrinsic viscosity, denaturation temperature and the thermodynamic parameters with the variation of concentration of catfish collagen were also thoroughly examined. The change of thermodynamic parameters from coiled-coil to random-coil conformation upon denaturation of collagen were calculated from the amount of proline and hydroxyproline residues and compared with viscometric results.
Full text
PDF
Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- Chiancone E., Gilbert G. A. Dissociation of hemoglobin into subunits. I. Oxyhemoglobin: effect of acetic acid. J Biol Chem. 1965 Oct;240(10):3866–3867. [PubMed] [Google Scholar]
- HARRINGTON W. F. ON THE ARRANGEMENT OF THE HYDROGEN BONDS IN THE STRUCTURE OF COLLAGEN. J Mol Biol. 1964 Aug;9:613–617. doi: 10.1016/s0022-2836(64)80234-5. [DOI] [PubMed] [Google Scholar]
- HARRINGTON W. F., SELA M. Studies on the structure of poly-L-proline in solution. Biochim Biophys Acta. 1958 Jan;27(1):24–41. doi: 10.1016/0006-3002(58)90289-0. [DOI] [PubMed] [Google Scholar]
- McClain P. E., Wiley E. R. Differential scanning calorimeter studies of the thermal transitions of collagen. Implications on structure and stability. J Biol Chem. 1972 Feb 10;247(3):692–697. [PubMed] [Google Scholar]
- Nicoli D. F., Benedek G. B. Study of thermal denaturation of lysozyme and other glubular proteins by light-scattering spectroscopy. Biopolymers. 1976 Dec;15(12NA-NA-770103-770104):2421–2437. doi: 10.1002/bip.1976.360151209. [DOI] [PubMed] [Google Scholar]
- PIEZ K. A., GROSS J. The amino acid composition of some fish collagens: the relation between composition and structure. J Biol Chem. 1960 Apr;235:995–998. [PubMed] [Google Scholar]
- Privalov P. L. Stability of proteins. Proteins which do not present a single cooperative system. Adv Protein Chem. 1982;35:1–104. [PubMed] [Google Scholar]
- Privalov P. L., Tiktopulo E. I. Thermal conformational transformation of tropocollagen. I. Calorimetric study. Biopolymers. 1970 Feb;9(2):127–139. doi: 10.1002/bip.1970.360090202. [DOI] [PubMed] [Google Scholar]
- Rigby B. J. Relation between the shrinkage of native collagen in acid solution and the melting temperature of the tropocollagen molecule. Biochim Biophys Acta. 1967 Feb 21;133(2):272–277. doi: 10.1016/0005-2795(67)90067-0. [DOI] [PubMed] [Google Scholar]