<Originals>Transition Temperature of Collagen Determined by ^1H-NMR

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概要

• 論文の詳細を見る

• The ^1H-NMR spectra of type I collagen from bovine aorta and rat tail tendon were measured at various temperatures from 6 to 60℃ in D_20 solution of 1 M NaCl at neutral pH. As the temperature increased, the collagen solution was transformed into gel. Further elevation of temperature caused the denaturation of collagen and gel was remelted to a clear solution. ^1H-NMR signals for Ala-β-CH_3 and a few other types of amino acid residues were hardly affected by the sol-gel transition. The intensities of ^1H-NMR signal increased dramatically by denaturation of collagen. Their transition temperatures were found at around 46℃ irrespective of amino acid residues referred. The detectable difference of denaturation temperature of collagens could not be observed between bovine aorta and rat tail tendon.

• 近畿大学の論文
• 1982-06-25

著者

• Asakura Jun-ichi

  First Department Of Biochemistry Kinki University School Of Medicine

• Shibata Susumu

  First Department Of Biochemistry Kinki University School Of Medicine

• ISEMURA Toshizo

  First Department of Biochemistry, Kinki University School of Medicine

• Isemura Toshizo

  First Department Of Biochemistry Kinki University School Of Medicine

関連論文

• Transition Temperature of Collagen Determined by ^1H-NMR

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