메뉴 건너뛰기




Volumn 60, Issue 2, 2007, Pages 213-220

A fluorescence spectroscopic study of a coagulating protein extracted from Moringa oleifera seeds

Author keywords

Helix; Coagulant protein; Ionic strength; Protein conformation; Quencher; Steady state fluorescence; Stern Volmer equation; Tryptophan

Indexed keywords

COAGULATION; FLUORESCENCE SPECTROSCOPY; IONIC STRENGTH; PH EFFECTS; QUENCHING; SEED;

EID: 35648974162     PISSN: 09277765     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.colsurfb.2007.06.015     Document Type: Article
Times cited : (60)

References (38)
  • 2
    • 0345676550 scopus 로고    scopus 로고
    • Quality of water treated by coagulation using Moringa oleifera seeds
    • Ndabigengesere A., and Narasiah K.S. Quality of water treated by coagulation using Moringa oleifera seeds. Water Res. 32 (1998) 781
    • (1998) Water Res. , vol.32 , pp. 781
    • Ndabigengesere, A.1    Narasiah, K.S.2
  • 3
    • 35649000743 scopus 로고    scopus 로고
    • L.J. Fuglie, The Miracle Tree Moringa oleifera, Natural nutrition for the tropics, Dakar, 1999.
  • 4
    • 35649008203 scopus 로고    scopus 로고
    • T.L. Hart, Natural coagulants: an investigation of Moringa oleifera and Tamarind seeds, M.Sc. Report, Texas, Austin, 2000.
  • 6
    • 35649015708 scopus 로고    scopus 로고
    • K.A. Ghebremichael, Moringa oleifera and Pumice as alternative natural materials for drinking water treatment, Ph.D. Thesis, Kungl Tekniska Högskolan, Stockholm, 2004.
  • 7
    • 35648987483 scopus 로고    scopus 로고
    • K. Levicki, A catchment to consumer approach to rural water resource assessment: baseline study and safe drinking supply strategy for Orongo village, Lake Victoria Basin, Kenya, M.Sc. Thesis, Stockholm, Sweden, 2005.
  • 8
    • 73949121499 scopus 로고    scopus 로고
    • Water clarification using Moringa oleifera seed coagulant
    • Shaw R. (Ed), Intermediate Technology Publications, London
    • Folkard G.K., Sutherland J.P., and Shaw R. Water clarification using Moringa oleifera seed coagulant. In: Shaw R. (Ed). Running Water (1999), Intermediate Technology Publications, London 1109-1112
    • (1999) Running Water , pp. 1109-1112
    • Folkard, G.K.1    Sutherland, J.P.2    Shaw, R.3
  • 9
    • 0025597710 scopus 로고
    • Natural coagulants for appropriate water treatment: a novel approach
    • Sutherland J.P., Folkard G.K., Mtawali M.A., and Grant W.D. Natural coagulants for appropriate water treatment: a novel approach. Waterlines 8 (1990) 30
    • (1990) Waterlines , vol.8 , pp. 30
    • Sutherland, J.P.1    Folkard, G.K.2    Mtawali, M.A.3    Grant, W.D.4
  • 10
    • 0028946850 scopus 로고
    • Isolation and characterization of a flocculating protein from Moringa oleifera Lam
    • Gassenschmidt U., Jany K.D., Tanscher B., and Niebergall H. Isolation and characterization of a flocculating protein from Moringa oleifera Lam. Biochim. Biophys. Acta 1243 (1995) 477
    • (1995) Biochim. Biophys. Acta , vol.1243 , pp. 477
    • Gassenschmidt, U.1    Jany, K.D.2    Tanscher, B.3    Niebergall, H.4
  • 11
    • 0029239595 scopus 로고
    • Active agents and mechanism coagulation of turbid waters using Moringa oleifera
    • Ndabigengesere A., Narasiah S., and Talbot B.G. Active agents and mechanism coagulation of turbid waters using Moringa oleifera. Water Res. 29 (1995) 703
    • (1995) Water Res. , vol.29 , pp. 703
    • Ndabigengesere, A.1    Narasiah, S.2    Talbot, B.G.3
  • 12
    • 0032722143 scopus 로고    scopus 로고
    • Improvement of extraction method of coagulation active components from Moringa oleifera seed
    • Okuda T., Baes A.U., Nishijima W., and Okada M. Improvement of extraction method of coagulation active components from Moringa oleifera seed. Water Res. 33 (1999) 3373
    • (1999) Water Res. , vol.33 , pp. 3373
    • Okuda, T.1    Baes, A.U.2    Nishijima, W.3    Okada, M.4
  • 13
    • 0035255730 scopus 로고    scopus 로고
    • Isolation and characterization of coagulant extracted from Moringa oleifera seed by salt solution
    • Okuda T., Baes A.U., Nishijima W., and Okada M. Isolation and characterization of coagulant extracted from Moringa oleifera seed by salt solution. Water Res. 35 (2001) 405
    • (2001) Water Res. , vol.35 , pp. 405
    • Okuda, T.1    Baes, A.U.2    Nishijima, W.3    Okada, M.4
  • 14
    • 20544434380 scopus 로고    scopus 로고
    • A simple purification and activity assay of the coagulant protein from Moringa oleifera seed
    • Ghebremichael K.A., Gunarutna K.R., Henrikson H., Brumer H., and Dalhammor G. A simple purification and activity assay of the coagulant protein from Moringa oleifera seed. Water Res. 39 (2005) 2338
    • (2005) Water Res. , vol.39 , pp. 2338
    • Ghebremichael, K.A.1    Gunarutna, K.R.2    Henrikson, H.3    Brumer, H.4    Dalhammor, G.5
  • 15
    • 33847010889 scopus 로고    scopus 로고
    • Interfacial properties and fluorescence of a coagulating protein extracted from Moringa oleifera seeds and its interaction with sodium dodecyl sulphate
    • Maikokera R., and Kwaambwa H.M. Interfacial properties and fluorescence of a coagulating protein extracted from Moringa oleifera seeds and its interaction with sodium dodecyl sulphate. Colloids Surf. B: Biointerfaces 55 (2007) 173
    • (2007) Colloids Surf. B: Biointerfaces , vol.55 , pp. 173
    • Maikokera, R.1    Kwaambwa, H.M.2
  • 16
    • 35648948228 scopus 로고    scopus 로고
    • D.L. Zeng, Investigation of protein-surfactant interactions in aqueous solutions, Ph.D. Thesis, The University of Connecticut, 1997.
  • 18
    • 77952957942 scopus 로고    scopus 로고
    • Proteins: some principles of classification and structure
    • Möbius D., and Miller R. (Eds), Elsevier Science B.V., Amsterdam
    • Schwenke K.D. Proteins: some principles of classification and structure. In: Möbius D., and Miller R. (Eds). Proteins at Liquid Interface (1998), Elsevier Science B.V., Amsterdam 1-50
    • (1998) Proteins at Liquid Interface , pp. 1-50
    • Schwenke, K.D.1
  • 19
    • 0033819120 scopus 로고    scopus 로고
    • States of tryptophyl residues and stability of recombinant human matrix metalloproteinase 7 (matrilysin) as examined by fluorescence
    • Inouye K., Tanaka H., and Oneda H. States of tryptophyl residues and stability of recombinant human matrix metalloproteinase 7 (matrilysin) as examined by fluorescence. J. Biochem. 128 (2000) 363
    • (2000) J. Biochem. , vol.128 , pp. 363
    • Inouye, K.1    Tanaka, H.2    Oneda, H.3
  • 20
    • 0034809210 scopus 로고    scopus 로고
    • Steady-state and time-resolved fluorescence studies on wild type and mutant Chromatium vinosum high potential iron proteins: halo- and apo-forms
    • Sau A.K., Chen C., Cowan J.A., Mazumdar S., and Mitra S. Steady-state and time-resolved fluorescence studies on wild type and mutant Chromatium vinosum high potential iron proteins: halo- and apo-forms. Biophys. J. 81 (2001) 2320
    • (2001) Biophys. J. , vol.81 , pp. 2320
    • Sau, A.K.1    Chen, C.2    Cowan, J.A.3    Mazumdar, S.4    Mitra, S.5
  • 23
    • 0000894107 scopus 로고
    • Functional attributes of protein isolates: foods
    • Franks F. (Ed), Humana Press, New Jersey
    • Myers C. Functional attributes of protein isolates: foods. In: Franks F. (Ed). Characterization of Proteins (1988), Humana Press, New Jersey
    • (1988) Characterization of Proteins
    • Myers, C.1
  • 24
    • 0028955635 scopus 로고
    • Fluorescence resolution of the intrinsic tryptophan residues of bovine protein tyrosyl phosphate
    • Pokalsky C., Wick P., Harms E., Lytle F.E., and Van Etten R.L. Fluorescence resolution of the intrinsic tryptophan residues of bovine protein tyrosyl phosphate. J. Biol. Chem. 270 (1995) 3809
    • (1995) J. Biol. Chem. , vol.270 , pp. 3809
    • Pokalsky, C.1    Wick, P.2    Harms, E.3    Lytle, F.E.4    Van Etten, R.L.5
  • 26
  • 27
    • 0033817980 scopus 로고    scopus 로고
    • Effect of a water extract of Moringa oleifera seeds on the hydrolytic microbial species diversity of a UASB reactor treating domestic wastewater
    • Kalogo Y., Rosillon F., Hammes F., and Verstraete W. Effect of a water extract of Moringa oleifera seeds on the hydrolytic microbial species diversity of a UASB reactor treating domestic wastewater. Lett. Appl. Microbiol. 31 (2000) 259
    • (2000) Lett. Appl. Microbiol. , vol.31 , pp. 259
    • Kalogo, Y.1    Rosillon, F.2    Hammes, F.3    Verstraete, W.4
  • 28
    • 0031687227 scopus 로고    scopus 로고
    • Fluorescence quenching and time-resolved fluorescence studies on Momordica charantia (Bitter Gourd) seed Lectin
    • Padma P., Komath S.S., and Swamy M.J. Fluorescence quenching and time-resolved fluorescence studies on Momordica charantia (Bitter Gourd) seed Lectin. Biochem. Mol. Biol. Int. 45 (1998) 911
    • (1998) Biochem. Mol. Biol. Int. , vol.45 , pp. 911
    • Padma, P.1    Komath, S.S.2    Swamy, M.J.3
  • 30
    • 0004135491 scopus 로고
    • Franks F. (Ed), Humana Press, New Jersey
    • In: Franks F. (Ed). Characterization of Proteins (1988), Humana Press, New Jersey
    • (1988) Characterization of Proteins
  • 32
    • 3242742115 scopus 로고    scopus 로고
    • The optimization of protein secondary structure determination with infrared and circular dichroism spectra
    • Oberg K.A., Ruysschaert J.M., and Goormaghtgh E. The optimization of protein secondary structure determination with infrared and circular dichroism spectra. Eur. J. Biochem. 271 (2004) 2937
    • (2004) Eur. J. Biochem. , vol.271 , pp. 2937
    • Oberg, K.A.1    Ruysschaert, J.M.2    Goormaghtgh, E.3
  • 34
    • 35648983836 scopus 로고    scopus 로고
    • J. Ravi, R. Tantra, A. Knight, Techniques for measurement of the structure of proteins in solution, and their complementary to circular dichroism, National Physical Laboratory report, DQL/AS/023, 2005, www.npl.co.uk, accessed in March 2006.
  • 35
    • 3543146731 scopus 로고    scopus 로고
    • Quenching of the intrinsic fluorescence of bovine serum albumin by chlorpromazine and hemin
    • Silva D., Cortez C.M., and Louro S.R.W. Quenching of the intrinsic fluorescence of bovine serum albumin by chlorpromazine and hemin. Braz. J. Med. Res. 37 (2004) 963
    • (2004) Braz. J. Med. Res. , vol.37 , pp. 963
    • Silva, D.1    Cortez, C.M.2    Louro, S.R.W.3
  • 36
    • 0023323198 scopus 로고
    • Studies on tryptophan residues of Abrus agglutinin; stopped-flow kinetics of modification and fluorescence quenching studies
    • Patanjali S.R., Swamy J.M., and Surolia A. Studies on tryptophan residues of Abrus agglutinin; stopped-flow kinetics of modification and fluorescence quenching studies. Biochem. J. 243 (1987) 79
    • (1987) Biochem. J. , vol.243 , pp. 79
    • Patanjali, S.R.1    Swamy, J.M.2    Surolia, A.3
  • 37
    • 0038793591 scopus 로고    scopus 로고
    • Surface changes and role of buried water molecules during the sulfane sulfur transfer in Rhodanese from Azotobactor vinelandii: a fluorescence quenching and nuclear magnetic relaxation dispersion spectroscopic study
    • Fasano M., Orsale M., Melino S., Nicolai E., Forlani F., Rosato N., Cicero D., Pagani S., and Paci M. Surface changes and role of buried water molecules during the sulfane sulfur transfer in Rhodanese from Azotobactor vinelandii: a fluorescence quenching and nuclear magnetic relaxation dispersion spectroscopic study. Biochemistry 42 (2003) 8550
    • (2003) Biochemistry , vol.42 , pp. 8550
    • Fasano, M.1    Orsale, M.2    Melino, S.3    Nicolai, E.4    Forlani, F.5    Rosato, N.6    Cicero, D.7    Pagani, S.8    Paci, M.9
  • 38
    • 20444504353 scopus 로고    scopus 로고
    • Acrylamide-quenching of Rhizomuco meihei lipase
    • Stobiecka A. Acrylamide-quenching of Rhizomuco meihei lipase. J. Photochem. Photobiol. B: Biol. 80 (2005) 9
    • (2005) J. Photochem. Photobiol. B: Biol. , vol.80 , pp. 9
    • Stobiecka, A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.