[Temperature dependence of the kinetics of renaturation of partially denatured collagen].
By the method of optical activity it has been studied the temperature dependence of the triple helical refolding process of partially denatured collagen from the skin and swim bladder of the mirror carp, and also that of the rat skin. It is shown that reducing the renaturation temperature the triple helical refolding rate increases and is in perfect agreement with the earlier observed fact [1,2]. The temperature coefficient of the reaction rate in the investigated region of temperatures remains constant, this fact ought to point to the zero value of activity energy of cis-trans isomerization process since renaturation goes on without nucleation stage. The obtained data do not agree with the earlier measured value of the activity energy of cis-trans isomerization process at collagen full denaturation [3-5].
Burdzhanadze
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Bezhitadze
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D000818:Animals; D003094:Collagen / Q000737:chemistry*; D005399:Fishes; D007700:Kinetics; D011489:Protein Denaturation; D051381:Rats; D013696:Temperature
D003094:Collagen