A comparative study of structural properties of fibronectin and its 180 kDa fragment

FEBS Letters

Koteliansky, V.E.¹  Morozkin, A.D.¹  Sepetov, N.F.¹  Metsis, M.L.¹  Bushuev, V.N.¹  Ruuge, E.K.¹ 

[1] Institute of Experimental Cardiology, USSR Cardiology Research Center, Academy of Medical Sciences, 3rd Cherepkovskaya Str. 15A, Block 7, 121552 Moscow, USSR

关键词: Fibronectin;    180 kDa fibronectin fragment;    1H-NMR;   

DOI  :  10.1016/0014-5793(85)81039-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Fibronectin from human plasma and its 180 kDa fragment which retained collagen-binding, cell-attachment and heparin-binding activities, were studied by velocity centrifugation and ¹H-NMR methods. The fibronectin hydrodynamic radius strongly increased at pH 11 while the hydrodynamic properties of the fragment did not change noticeably. ¹H-NMR spectroscopy also showed differences in the molecular properties of fibronectin and its 180 kDa fragment. Under physiological conditions the structure of fibronectin differs from that of its 180 kDa fragment. At pH 11 and in 4 M urea no differences in their structures are observed. It is suggested that interdomain and intersubunit interactions play an important role in maintaining the native conformation of intact fibronectin.

【 授权许可】

Unknown