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Renaturation of α1 Chains from Shark Skin Collagen Type 1
Author(s) -
NOMURA YOSHIHIRO,
YAMANO MASAYA,
SHIRAI KUNIO
Publication year - 1995
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1365-2621.1995.tb04563.x
Subject(s) - viscosity , chemistry , rotation (mathematics) , optical rotation , intrinsic viscosity , chain (unit) , biophysics , constant (computer programming) , crystallography , polymer chemistry , chromatography , materials science , organic chemistry , polymer , biology , composite material , mathematics , geometry , astronomy , physics , computer science , programming language
Renaturation of α1 chains from shark skin collagen (1) was measured by the increase in optical rotation and viscosity. The rotation change of the α1(1) chains became constant after 18 hr, while the viscosity increased further with time. Size exclusion chromatographic patterns of renaturation products of α1 (I) chain gave similar results to that of native collagen. The renaturation products remelted with rising temperature in a similar way to the melting of native collagen as judged from the rotation‐temperature curve.
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