Big Chemical Encyclopedia

Chemical substances, components, reactions, process design ...

Articles Figures Tables About

Temperature collagen

Yunoki, S., Suzuki, T., and Takai, M. (2003). Stabilization of low denaturation temperature collagen from fish by physical cross-linking methods. J. Biosci. Bioeng. 96, 575-577. [Pg.120]

Fig. 23. Specific rotation of ichthyocol collagen and gelatin at 313 wn as a function of temperature. Collagen concentration = 1.14 mg/ml, gelatin concentration = 1.67 mg/ml. T, gelatin, after 24 hr at 3°C A, gelatin after 6 days at 3°C O, gelatin after 28 days at 3°C O, native soluble collagen. (From Harrington and von Hippel, 1961.)... Fig. 23. Specific rotation of ichthyocol collagen and gelatin at 313 wn as a function of temperature. Collagen concentration = 1.14 mg/ml, gelatin concentration = 1.67 mg/ml. T, gelatin, after 24 hr at 3°C A, gelatin after 6 days at 3°C O, gelatin after 28 days at 3°C O, native soluble collagen. (From Harrington and von Hippel, 1961.)...
Table 5. Formation of the negatively and positive sequences in water and methanol, indicated by the collagen-like CD spectra and by the shape of the temperature transition curve... Table 5. Formation of the negatively and positive sequences in water and methanol, indicated by the collagen-like CD spectra and by the shape of the temperature transition curve...
Cohen (4) has suggested that the high equilibrium specific rotation of gelatin at low temperature is due to a partial regaining of the helical structure of collagen. In order to regain such a structure, it would be necessary to impose severe restrictions on the molecule. As pointed out by Ferry and Eldridge (5),... [Pg.34]

The Pn conformation of poly-L-proline (PP) or collagen in the solid state could be identified from X-ray fiber diffraction results (Cowan and McGavin, 1955). Persistence of this basic structure in solution was inferred from the resemblance between the CD spectra of solutions and films of the polypeptide. The CD spectra of the charged forms of PGA and PL closely resemble that of Pn (compare Fig. IB, 1C, and ID) however, these spectra differ significantly from those of PP peptides at high temperature or in the presence of high concentration of salts... [Pg.188]


See other pages where Temperature collagen is mentioned: [Pg.177]    [Pg.806]    [Pg.319]    [Pg.273]    [Pg.161]    [Pg.426]    [Pg.145]    [Pg.310]    [Pg.177]    [Pg.806]    [Pg.319]    [Pg.273]    [Pg.161]    [Pg.426]    [Pg.145]    [Pg.310]    [Pg.164]    [Pg.165]    [Pg.1116]    [Pg.164]    [Pg.172]    [Pg.179]    [Pg.179]    [Pg.180]    [Pg.173]    [Pg.73]    [Pg.148]    [Pg.243]    [Pg.249]    [Pg.250]    [Pg.85]    [Pg.144]    [Pg.149]    [Pg.152]    [Pg.154]    [Pg.162]    [Pg.162]    [Pg.119]    [Pg.24]    [Pg.462]    [Pg.249]    [Pg.198]    [Pg.445]    [Pg.499]    [Pg.327]    [Pg.350]    [Pg.353]    [Pg.360]    [Pg.361]    [Pg.192]   
See also in sourсe #XX -- [ Pg.166 ]

See also in sourсe #XX -- [ Pg.15 ]




SEARCH



Collagen fish, shrinkage temperature

Collagen glass transition temperature

Collagen shrinkage temperature

Collagen, melting temperature

Melting temperature of collagen

© 2024 chempedia.info