Literature DB >> 3342002

A study of the hydration and thermodynamics of warm-water and cold-water fish collagens.

C Rose1, M Kumar, A B Mandal.   

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.

Entities:  

Mesh:

Substances:

Year:  1988        PMID: 3342002      PMCID: PMC1148675          DOI: 10.1042/bj2490127

Source DB:  PubMed          Journal:  Biochem J        ISSN: 0264-6021            Impact factor:   3.857


  9 in total

1.  ON THE ARRANGEMENT OF THE HYDROGEN BONDS IN THE STRUCTURE OF COLLAGEN.

Authors:  W F HARRINGTON
Journal:  J Mol Biol       Date:  1964-08       Impact factor: 5.469

2.  The amino acid composition of some fish collagens: the relation between composition and structure.

Authors:  K A PIEZ; J GROSS
Journal:  J Biol Chem       Date:  1960-04       Impact factor: 5.157

3.  Studies on the structure of poly-L-proline in solution.

Authors:  W F HARRINGTON; M SELA
Journal:  Biochim Biophys Acta       Date:  1958-01

4.  Study of thermal denaturation of lysozyme and other glubular proteins by light-scattering spectroscopy.

Authors:  D F Nicoli; G B Benedek
Journal:  Biopolymers       Date:  1976-12       Impact factor: 2.505

5.  Differential scanning calorimeter studies of the thermal transitions of collagen. Implications on structure and stability.

Authors:  P E McClain; E R Wiley
Journal:  J Biol Chem       Date:  1972-02-10       Impact factor: 5.157

6.  Thermal conformational transformation of tropocollagen. I. Calorimetric study.

Authors:  P L Privalov; E I Tiktopulo
Journal:  Biopolymers       Date:  1970-02       Impact factor: 2.505

7.  Dissociation of hemoglobin into subunits. I. Oxyhemoglobin: effect of acetic acid.

Authors:  E Chiancone; G A Gilbert
Journal:  J Biol Chem       Date:  1965-10       Impact factor: 5.157

Review 8.  Stability of proteins. Proteins which do not present a single cooperative system.

Authors:  P L Privalov
Journal:  Adv Protein Chem       Date:  1982

9.  Relation between the shrinkage of native collagen in acid solution and the melting temperature of the tropocollagen molecule.

Authors:  B J Rigby
Journal:  Biochim Biophys Acta       Date:  1967-02-21
  9 in total
  2 in total

1.  Purification, crystallization, preliminary X-ray diffraction and molecular-replacement studies of catfish (Clarias magur) haemoglobin.

Authors:  S M Jaimohan; M D Naresh; A B Mandal
Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun       Date:  2012-10-30

2.  Dentin collagen denaturation status assessed by collagen hybridizing peptide and its effect on bio-stabilization of proanthocyanidins.

Authors:  Rong Wang; Saleha Nisar; Zachary Vogel; Hang Liu; Yong Wang
Journal:  Dent Mater       Date:  2022-04-14       Impact factor: 5.687

  2 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.