메뉴 건너뛰기




Volumn 79, Issue 3, 2000, Pages 245-257

Isinglass/collagen: Denaturation and functionality

Author keywords

Clarification; Collagen; Denaturation; Isinglass

Indexed keywords

ALCOHOL; CHELATING AGENT; COLLAGEN; DETERGENT; HYDROXYL GROUP; HYDROXYPROLINE; ISINGLASS; MEMBRANE PROTEIN; PROTEIN; UNCLASSIFIED DRUG;

EID: 0034717159     PISSN: 01681656     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0168-1656(00)00241-8     Document Type: Conference Paper
Times cited : (78)

References (22)
  • 1
    • 0028873846 scopus 로고
    • Non-enzymic glycation of fibrous collagen - reaction products of glucose and ribose
    • Bailey A.J., Sims T.J., Avery N.C., Halligan E.P. Non-enzymic glycation of fibrous collagen - reaction products of glucose and ribose. Biochem. J. 305:1995;385-390.
    • (1995) Biochem. J. , vol.305 , pp. 385-390
    • Bailey, A.J.1    Sims, T.J.2    Avery, N.C.3    Halligan, E.P.4
  • 3
    • 0029645406 scopus 로고
    • Hydration structure of a collagen peptide
    • Bella J., Brodsky B., Berman H.M. Hydration structure of a collagen peptide. Structure. 3:1995;893-906.
    • (1995) Structure , vol.3 , pp. 893-906
    • Bella, J.1    Brodsky, B.2    Berman, H.M.3
  • 4
    • 0026908646 scopus 로고
    • Thermodynamic substantiation of water-bridged collagen structure
    • Burjanadze T. Thermodynamic substantiation of water-bridged collagen structure. Biopolymers. 32:1992;941-949.
    • (1992) Biopolymers , vol.32 , pp. 941-949
    • Burjanadze, T.1
  • 5
    • 26744450733 scopus 로고
    • Basic protein and peptide protocols
    • J.M. Walker. Totowa, NJ, USA: Humana Press
    • Carne A.F. Basic protein and peptide protocols. Walker J.M. Methods in Molecular Biology. 1994;Humana Press, Totowa, NJ, USA.
    • (1994) Methods in Molecular Biology
    • Carne, A.F.1
  • 7
    • 0017610806 scopus 로고
    • The triple helix-coil conversion of collagen-like polytripeptides in aqueous and non-aqueous solvents
    • Engel J., Chem H., Prockop D.J., Klump H. The triple helix-coil conversion of collagen-like polytripeptides in aqueous and non-aqueous solvents. Biopolymers. 16:1977;601-622.
    • (1977) Biopolymers , vol.16 , pp. 601-622
    • Engel, J.1    Chem, H.2    Prockop, D.J.3    Klump, H.4
  • 8
    • 0001032438 scopus 로고
    • Phase transitions in collagen and gelatin systems
    • Flory P.J., Garrett R.R. Phase transitions in collagen and gelatin systems. J. Am. Chem. Soc. 80:1958;4836-4845.
    • (1958) J. Am. Chem. Soc. , vol.80 , pp. 4836-4845
    • Flory, P.J.1    Garrett, R.R.2
  • 9
    • 0018400235 scopus 로고
    • Chain conformation in the collagen molecule
    • Fraser R.B.D., MacRae T.P., Suzuki E. Chain conformation in the collagen molecule. J. Mol. Biol. 129:1979;463-486.
    • (1979) J. Mol. Biol. , vol.129 , pp. 463-486
    • Fraser, R.B.D.1    MacRae, T.P.2    Suzuki, E.3
  • 10
    • 0000706840 scopus 로고
    • Estimation of hydroxyproline by the auto-analyser
    • Grant R.A. Estimation of hydroxyproline by the auto-analyser. J. Clin. Pathol. 17:1964;685-686.
    • (1964) J. Clin. Pathol. , vol.17 , pp. 685-686
    • Grant, R.A.1
  • 12
    • 0027213275 scopus 로고
    • Adherence of Candida albicans to immobilised extracellular matrix proteins is mediated by calcium-dependant surface glycoproteins
    • Klotz S.A., Rutten M.J., Smith R.L., Babcock S.R., Cunningham M.D. Adherence of Candida albicans to immobilised extracellular matrix proteins is mediated by calcium-dependant surface glycoproteins. Microbial Pathog. 14:1993;133-147.
    • (1993) Microbial Pathog. , vol.14 , pp. 133-147
    • Klotz, S.A.1    Rutten, M.J.2    Smith, R.L.3    Babcock, S.R.4    Cunningham, M.D.5
  • 13
    • 0028918983 scopus 로고
    • The kinetics of the thermal denaturation of collagen in unrestrained rat tail tendon determined by differential scanning calorimetry
    • Miles C.A., Burjanadze T.V., Bailey A.J. The kinetics of the thermal denaturation of collagen in unrestrained rat tail tendon determined by differential scanning calorimetry. J. Mol. Biol. 245:1995;437-446.
    • (1995) J. Mol. Biol. , vol.245 , pp. 437-446
    • Miles, C.A.1    Burjanadze, T.V.2    Bailey, A.J.3
  • 14
    • 0028997468 scopus 로고
    • Adherence of Candida albicans to host cells
    • Pendrak M.L., Klotz S.A. Adherence of Candida albicans to host cells. FEMS Microbiol. Lett. 129:1995;103-114.
    • (1995) FEMS Microbiol. Lett. , vol.129 , pp. 103-114
    • Pendrak, M.L.1    Klotz, S.A.2
  • 15
    • 0018588511 scopus 로고
    • Stability of proteins
    • Privalov P.L. Stability of proteins. Adv. Protein Chem. 33:1979;167-241.
    • (1979) Adv. Protein Chem. , vol.33 , pp. 167-241
    • Privalov, P.L.1
  • 16
    • 0015852842 scopus 로고
    • A hypothesis on the role of hydroxyproline in stabilising collagen structure
    • Ramachandran G.N., Bansal M., Bhastnagar R.S. A hypothesis on the role of hydroxyproline in stabilising collagen structure. Biochem. Biophys. Acta. 323:1973;166-171.
    • (1973) Biochem. Biophys. Acta , vol.323 , pp. 166-171
    • Ramachandran, G.N.1    Bansal, M.2    Bhastnagar, R.S.3
  • 17
    • 0343179543 scopus 로고
    • Isinglass Re-evaluated
    • October 32-38
    • Side, C.E., 1982. Isinglass Re-evaluated. Brewers Digest. October 32-38.
    • (1982) Brewers Digest.
    • Side, C.E.1
  • 18
    • 0026464899 scopus 로고
    • Quantitative analysis of collagen and elastin cross-links using a single column system
    • Sims T.J., Bailey A.J. Quantitative analysis of collagen and elastin cross-links using a single column system. J. Chromatog. 582:1992;49-55.
    • (1992) J. Chromatog. , vol.582 , pp. 49-55
    • Sims, T.J.1    Bailey, A.J.2
  • 19
    • 0026731606 scopus 로고
    • Yeast flocculation - receptor definition by MNN mutants and concanavalin-A
    • Stratford M. Yeast flocculation - receptor definition by MNN mutants and concanavalin-A. Yeast. 8:1992;635-645.
    • (1992) Yeast , vol.8 , pp. 635-645
    • Stratford, M.1
  • 20
    • 84987284112 scopus 로고
    • Some sterochemical implications of the molecular composition of collagen
    • Traub W. Some sterochemical implications of the molecular composition of collagen. Isr. J. Chem. 12:1974;435-439.
    • (1974) Isr. J. Chem. , vol.12 , pp. 435-439
    • Traub, W.1
  • 21
    • 0029928756 scopus 로고    scopus 로고
    • The effect of deamination and/or blocking arginine residues on the molecular assembly of acid-extracted rat tail tendon collagen
    • Wen Hu X., Knight D.P., Grant R.A. The effect of deamination and/or blocking arginine residues on the molecular assembly of acid-extracted rat tail tendon collagen. Tissue Cell. 28:1996;215-222.
    • (1996) Tissue Cell , vol.28 , pp. 215-222
    • Wen Hu, X.1    Knight, D.P.2    Grant, R.A.3
  • 22
    • 0018070633 scopus 로고
    • Collagen induced platelet aggregation and release. II. Critical size and structural requirements of collagen
    • Wang C.-L., Miyata T., Weksler B., Rubin A.L., Stenzel K.H. Collagen induced platelet aggregation and release. II. Critical size and structural requirements of collagen. Biochim. Biophys. Acta. 544:1978;555-567.
    • (1978) Biochim. Biophys. Acta , vol.544 , pp. 555-567
    • Wang, C.-L.1    Miyata, T.2    Weksler, B.3    Rubin, A.L.4    Stenzel, K.H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.