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Volumn 92, Issue 9, 1997, Pages 225-232

A conformational study of collagen as affected by tanning procedures

Author keywords

[No Author keywords available]

Indexed keywords

CARBOXYLIC ACIDS; CHROMIUM COMPOUNDS; CONFORMATIONS; CROSSLINKING; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; ORGANOMETALLICS; TANNING; TRANSMISSION ELECTRON MICROSCOPY;

EID: 0031276428     PISSN: 00029726     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (43)

References (14)
  • 1
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    • Molecular and aggregate structures of the collagens
    • K. A. Piez and A. H. Reddi eds. Elsevier, New York
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    • (1984) Extracelluar Matrix Biochemistry
    • Piez, K.A.1
  • 2
    • 0017343257 scopus 로고
    • Chemistry of the crosslinking of collagen during tanning
    • M. Friedman ed. Advances in Experimental Medicine and Biology
    • Harlan, J. W. and Feairheller, S. H.; Chemistry of the crosslinking of collagen during tanning. in Protein Crosslinking: Biochemical and Molecular Aspects, (M. Friedman ed.) Advances in Experimental Medicine and Biology, Vol. 86A pp. 425-440, 1977.
    • (1977) Protein Crosslinking: Biochemical and Molecular Aspects , vol.86 A , pp. 425-440
    • Harlan, J.W.1    Feairheller, S.H.2
  • 3
    • 0142159287 scopus 로고    scopus 로고
    • Review of chrome tanning. Part 1
    • 17-26, March
    • Chagne, V., Silvestre, F., and Gaset, A.; Review of chrome tanning. Part 1, Leather, 17-26, March 1996.
    • (1996) Leather
    • Chagne, V.1    Silvestre, F.2    Gaset, A.3
  • 4
    • 84987349261 scopus 로고
    • Solubilization of collagen in restructured beef with collagenases and α-amlyase
    • Cronlund, A. L., and Woychik J. H.; Solubilization of collagen in restructured beef with collagenases and α-amlyase. J. Food Sci. 52, 857-860, 1987.
    • (1987) J. Food Sci. , vol.52 , pp. 857-860
    • Cronlund, A.L.1    Woychik, J.H.2
  • 5
    • 0018079235 scopus 로고
    • Collagen fibril formation: Optimal invitro conditions and preliminary kinetic results
    • Williams, B. R., Gelman, R. A., Poppke, D. C. and Piez, K. A.; Collagen fibril formation: Optimal invitro conditions and preliminary kinetic results. J. Biol. Chem. 253, 6578-6585, 1978.
    • (1978) J. Biol. Chem. , vol.253 , pp. 6578-6585
    • Williams, B.R.1    Gelman, R.A.2    Poppke, D.C.3    Piez, K.A.4
  • 7
    • 0024046860 scopus 로고
    • UV Spectroscopic characterization of type I collagen
    • Na, G.C.; UV Spectroscopic characterization of type I collagen. Collagen Rel. Res. 8, 315(330, 1988.
    • (1988) Collagen Rel. Res. , vol.8 , pp. 315-330
    • Na, G.C.1
  • 8
    • 6044260625 scopus 로고    scopus 로고
    • Algorithm provided by Aviv Associates with the Model 60DS spectropolarimeter
    • Algorithm provided by Aviv Associates with the Model 60DS spectropolarimeter.
  • 9
    • 0008632507 scopus 로고
    • Carbon-13 chemical shift parameters for amines, carboxylic acids, and amino acids
    • Rabenstein, D.L. and Sayer, T.L.; Carbon-13 chemical shift parameters for amines, carboxylic acids, and amino acids. J. Magn. Reson. 24, 27-39, 1976.
    • (1976) J. Magn. Reson. , vol.24 , pp. 27-39
    • Rabenstein, D.L.1    Sayer, T.L.2
  • 11
    • 0014944058 scopus 로고
    • Characterization of the product formed by renaturation of αl-CB2, a small peptide from collagen
    • Piez, K. A. and Sherman, M. R.; Characterization of the product formed by renaturation of αl-CB2, a small peptide from collagen. Biochemistry 9, 4129-4133, 1970.
    • (1970) Biochemistry , vol.9 , pp. 4129-4133
    • Piez, K.A.1    Sherman, M.R.2
  • 12
    • 0015892994 scopus 로고
    • Analysis of the primary structure of collagen for the origins of molecular packing
    • Hulmes, D. J. S., Miller A., Parry, D. A. D., Piez, K. A. and Woodhead-Galloway, J.; Analysis of the primary structure of collagen for the origins of molecular packing. J. Mol. Biol. 79, 137-148, 1973.
    • (1973) J. Mol. Biol. , vol.79 , pp. 137-148
    • Hulmes, D.J.S.1    Miller, A.2    Parry, D.A.D.3    Piez, K.A.4    Woodhead-Galloway, J.5
  • 13
    • 0009658994 scopus 로고
    • Three-dimensional-energy minimized models for calf skin type I collagen triple helix and microfibril: I. the triple helical models
    • Chen, J. M., Feairheller, S. H. and Brown, E. M.; Three-dimensional-energy minimized models for calf skin type I collagen triple helix and microfibril: I. the triple helical models. JALCA 86, 475-486, 1991.
    • (1991) JALCA , vol.86 , pp. 475-486
    • Chen, J.M.1    Feairheller, S.H.2    Brown, E.M.3
  • 14
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    • Computer model of a bovine type I collagen microfibril
    • King, G., Brown, E. M., and Chen, J. M.; Computer model of a bovine type I collagen microfibril. Protein Engineering 9, 43-49, 1996.
    • (1996) Protein Engineering , vol.9 , pp. 43-49
    • King, G.1    Brown, E.M.2    Chen, J.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.