메뉴 건너뛰기




Volumn 51, Issue 10, 2006, Pages 861-869

Influences of animal mucins on lysozyme activity in solution and on hydroxyapatite surfaces

Author keywords

Bovine submaxillary mucin; Lysozyme; Porcine gastric mucin; Saliva

Indexed keywords

ENZYME INHIBITOR; HEN EGG LYSOZYME; HYDROXYAPATITE; LYSOZYME; MICROSPHERE; MUCIN;

EID: 33748523049     PISSN: 00039969     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.archoralbio.2006.04.002     Document Type: Article
Times cited : (19)

References (58)
  • 1
    • 0027313501 scopus 로고
    • Development of artificial salivas
    • Levine M.J. Development of artificial salivas. Crit Rev Oral Biol Med 4 (1993) 279-286
    • (1993) Crit Rev Oral Biol Med , vol.4 , pp. 279-286
    • Levine, M.J.1
  • 2
    • 0016279539 scopus 로고
    • The effect of mucin-containing artificial saliva on severe xerostomia
    • 's-Gravenmade E.J., Poukema P.A., and Panders A.K. The effect of mucin-containing artificial saliva on severe xerostomia. Int J Oral Surg 3 (1974) 435-439
    • (1974) Int J Oral Surg , vol.3 , pp. 435-439
    • 's-Gravenmade, E.J.1    Poukema, P.A.2    Panders, A.K.3
  • 3
    • 0017664225 scopus 로고
    • A saliva substitute for use by xerostomic patients undergoing radiotherapy to the head and neck
    • Shannon I.L., McCrary B.R., and Starcke E.N. A saliva substitute for use by xerostomic patients undergoing radiotherapy to the head and neck. Oral Surg 44 (1977) 656-661
    • (1977) Oral Surg , vol.44 , pp. 656-661
    • Shannon, I.L.1    McCrary, B.R.2    Starcke, E.N.3
  • 4
    • 0020800795 scopus 로고
    • A clinical comparison between commercially available mucin- and CMC-containing saliva substitutes
    • Vissink A., 's-Gravenmade E.J., Panders A.K., et al. A clinical comparison between commercially available mucin- and CMC-containing saliva substitutes. Int J Oral Surg 12 (1983) 232-238
    • (1983) Int J Oral Surg , vol.12 , pp. 232-238
    • Vissink, A.1    's-Gravenmade, E.J.2    Panders, A.K.3
  • 7
    • 0024977974 scopus 로고
    • A double-blind cross-over trial of a mucin-containing artificial saliva
    • Duxbury A.J., Thakker N.S., and Wastell D.G. A double-blind cross-over trial of a mucin-containing artificial saliva. Br Dent J 166 (1989) 115-120
    • (1989) Br Dent J , vol.166 , pp. 115-120
    • Duxbury, A.J.1    Thakker, N.S.2    Wastell, D.G.3
  • 8
    • 0020197980 scopus 로고
    • Purification of a low-molecular weight mucin type glycoprotein from human submandibular-sublingual saliva
    • Prakobphol A., Levine M.J., Tabak L.A., and Reddy M.A. Purification of a low-molecular weight mucin type glycoprotein from human submandibular-sublingual saliva. Carbohydr Res 108 (1982) 111-122
    • (1982) Carbohydr Res , vol.108 , pp. 111-122
    • Prakobphol, A.1    Levine, M.J.2    Tabak, L.A.3    Reddy, M.A.4
  • 9
    • 0020174087 scopus 로고
    • The isolation of a family of cysteine-containing phosphoproteins from human submandibular-sublingual saliva
    • Shomers J.P., Tabak L.A., Levine M.J., Mandel I.D., and Ellison S.A. The isolation of a family of cysteine-containing phosphoproteins from human submandibular-sublingual saliva. J Dent Res 61 (1982) 973-977
    • (1982) J Dent Res , vol.61 , pp. 973-977
    • Shomers, J.P.1    Tabak, L.A.2    Levine, M.J.3    Mandel, I.D.4    Ellison, S.A.5
  • 10
    • 0023203158 scopus 로고
    • Biochemical and biophysical comparison of two mucins from human submandibular-sublingual saliva
    • Loomis R.E., Prakobphol A., Levine M.J., Reddy M.S., and Jones P.C. Biochemical and biophysical comparison of two mucins from human submandibular-sublingual saliva. Arch Biochem Biophys 258 (1987) 452-464
    • (1987) Arch Biochem Biophys , vol.258 , pp. 452-464
    • Loomis, R.E.1    Prakobphol, A.2    Levine, M.J.3    Reddy, M.S.4    Jones, P.C.5
  • 11
    • 0026094266 scopus 로고
    • Interaction of a salivary mucin-secretory immunoglobulin A complex with mucosal pathogens
    • Biesbrock A.R., Reddy M.S., and Levine M.J. Interaction of a salivary mucin-secretory immunoglobulin A complex with mucosal pathogens. Infect Immun 59 (1991) 3492-3497
    • (1991) Infect Immun , vol.59 , pp. 3492-3497
    • Biesbrock, A.R.1    Reddy, M.S.2    Levine, M.J.3
  • 12
    • 0031089153 scopus 로고    scopus 로고
    • Human salivary mucin MG1 selectively forms heterotypic complexes with amylase, proline-rich proteins, statherin, and histatins
    • Iontcheva I., Oppenheim F.G., and Troxler R.F. Human salivary mucin MG1 selectively forms heterotypic complexes with amylase, proline-rich proteins, statherin, and histatins. J Dent Res 76 (1997) 734-743
    • (1997) J Dent Res , vol.76 , pp. 734-743
    • Iontcheva, I.1    Oppenheim, F.G.2    Troxler, R.F.3
  • 14
    • 0035676981 scopus 로고    scopus 로고
    • Identification of a nonmucin glycoprotein (gp-340) from a purified respiratory mucin preparation: evidence for an association involving the MUC5B mucin
    • Thornton D.J., Davies J.R., Kirkham S., et al. Identification of a nonmucin glycoprotein (gp-340) from a purified respiratory mucin preparation: evidence for an association involving the MUC5B mucin. Glycobiology 11 (2001) 969-977
    • (2001) Glycobiology , vol.11 , pp. 969-977
    • Thornton, D.J.1    Davies, J.R.2    Kirkham, S.3
  • 15
    • 0014960645 scopus 로고
    • Structural studies on gastric mucoproteins; lowering of molecular weight after reduction with 2-mercaptoethanol
    • Snary D., Allen A., and Pain R.H. Structural studies on gastric mucoproteins; lowering of molecular weight after reduction with 2-mercaptoethanol. Biochem Biophys Res Commun 40 (1970) 844-851
    • (1970) Biochem Biophys Res Commun , vol.40 , pp. 844-851
    • Snary, D.1    Allen, A.2    Pain, R.H.3
  • 17
    • 0030867473 scopus 로고    scopus 로고
    • Mucus glycoproteins from pig gastric mucosa: identification of different mucin populations from the surface epithelium
    • Nordman H., Davies J.R., Herrmann A., Karlsson N.G., Hansson G.C., and Carlstedt I. Mucus glycoproteins from pig gastric mucosa: identification of different mucin populations from the surface epithelium. Biochem J 326 (1997) 903-910
    • (1997) Biochem J , vol.326 , pp. 903-910
    • Nordman, H.1    Davies, J.R.2    Herrmann, A.3    Karlsson, N.G.4    Hansson, G.C.5    Carlstedt, I.6
  • 18
    • 0034052605 scopus 로고    scopus 로고
    • The central domain of bovine submaxillary mucin consists of over 50 tandem repeats of 329 amino acids. Chromosomal localization of the BSM1 gene and relations to ovine and porcine counterparts
    • Jiang W., Gupta D., Gallagher D., Davis S., and Bhavanandan V.P. The central domain of bovine submaxillary mucin consists of over 50 tandem repeats of 329 amino acids. Chromosomal localization of the BSM1 gene and relations to ovine and porcine counterparts. Eur J Biochem 267 (2000) 2208-2217
    • (2000) Eur J Biochem , vol.267 , pp. 2208-2217
    • Jiang, W.1    Gupta, D.2    Gallagher, D.3    Davis, S.4    Bhavanandan, V.P.5
  • 19
    • 0021490172 scopus 로고
    • What's new in lysozyme research? Always a model system, today as yesterday
    • Jolles P., and Jolles J. What's new in lysozyme research? Always a model system, today as yesterday. Mol Cell Biochem 63 (1984) 165-189
    • (1984) Mol Cell Biochem , vol.63 , pp. 165-189
    • Jolles, P.1    Jolles, J.2
  • 20
    • 0021796925 scopus 로고
    • Bactericidal activity of human lysozyme, muramidase-inactive lysozyme, and cationic polypeptides against Streptococcus sanguis and Streptococcus faecalis: inhibition by chitin oligosaccharides
    • Laible N.J., and Germaine G.R. Bactericidal activity of human lysozyme, muramidase-inactive lysozyme, and cationic polypeptides against Streptococcus sanguis and Streptococcus faecalis: inhibition by chitin oligosaccharides. Infect Immun 48 (1985) 720-728
    • (1985) Infect Immun , vol.48 , pp. 720-728
    • Laible, N.J.1    Germaine, G.R.2
  • 21
    • 0035964823 scopus 로고    scopus 로고
    • Genetic evidence that antibacterial activity of lysozyme is independent of its catalytic function
    • Ibrahim H.R., Matsuzaki T., and Aoki T. Genetic evidence that antibacterial activity of lysozyme is independent of its catalytic function. FEBS Lett 506 (2001) 27-32
    • (2001) FEBS Lett , vol.506 , pp. 27-32
    • Ibrahim, H.R.1    Matsuzaki, T.2    Aoki, T.3
  • 23
    • 0023852850 scopus 로고
    • Conformational states of enzymes bound to surfaces
    • Sandwick T.K., and Schray K.J. Conformational states of enzymes bound to surfaces. J Colloid Interface Sci 121 (1988) 1-12
    • (1988) J Colloid Interface Sci , vol.121 , pp. 1-12
    • Sandwick, T.K.1    Schray, K.J.2
  • 25
    • 0023849753 scopus 로고
    • Human salivary acidic proline-rich proteins and statherin promote the attachment of Actinomyces viscosus LY7 to apatitic surfaces
    • Gibbons R.J., and Hay D.I. Human salivary acidic proline-rich proteins and statherin promote the attachment of Actinomyces viscosus LY7 to apatitic surfaces. Infect Immun 56 (1988) 439-445
    • (1988) Infect Immun , vol.56 , pp. 439-445
    • Gibbons, R.J.1    Hay, D.I.2
  • 26
    • 0025886803 scopus 로고
    • Delineation of a segment of absorbed salivary acidic proline-rich proteins which promotes adhesion of Streptococcus gordonii to apatite surfaces
    • Gibbons R.J., Hay D.I., and Schlesinger D.H. Delineation of a segment of absorbed salivary acidic proline-rich proteins which promotes adhesion of Streptococcus gordonii to apatite surfaces. Infect Immun 59 (1991) 2948-2954
    • (1991) Infect Immun , vol.59 , pp. 2948-2954
    • Gibbons, R.J.1    Hay, D.I.2    Schlesinger, D.H.3
  • 27
    • 14644439885 scopus 로고    scopus 로고
    • Enzymes in the acquired enamel pellicle
    • Hannig C., Hannig M., and Attin T. Enzymes in the acquired enamel pellicle. Eur J Oral Sci 113 (2005) 2-13
    • (2005) Eur J Oral Sci , vol.113 , pp. 2-13
    • Hannig, C.1    Hannig, M.2    Attin, T.3
  • 28
    • 0023952622 scopus 로고
    • The activity of glucosyltransferase adsorbed onto saliva-coated hydroxyapatite
    • Schilling K.M., and Bowen W.H. The activity of glucosyltransferase adsorbed onto saliva-coated hydroxyapatite. J Dent Res 67 (1988) 2-8
    • (1988) J Dent Res , vol.67 , pp. 2-8
    • Schilling, K.M.1    Bowen, W.H.2
  • 29
    • 0030099910 scopus 로고    scopus 로고
    • Interactions of streptococcal glucosyltransferases with α-amylase and starch on the surface of saliva-coated hydroxyapatite
    • Vacca-Smith A.M., Venkitaraman A.R., Quivey R.G., and Bowen W.H. Interactions of streptococcal glucosyltransferases with α-amylase and starch on the surface of saliva-coated hydroxyapatite. Arch Oral Biol 41 (1996) 291-298
    • (1996) Arch Oral Biol , vol.41 , pp. 291-298
    • Vacca-Smith, A.M.1    Venkitaraman, A.R.2    Quivey, R.G.3    Bowen, W.H.4
  • 30
    • 0030332898 scopus 로고    scopus 로고
    • Characterization of glucosyltransferase of human saliva adsorbed on to hydroxyapatite surfaces
    • Vacca-Smith A.M., Venkitaraman A.R., Schilling K.M., and Bowen W.H. Characterization of glucosyltransferase of human saliva adsorbed on to hydroxyapatite surfaces. Caries Res 30 (1996) 354-360
    • (1996) Caries Res , vol.30 , pp. 354-360
    • Vacca-Smith, A.M.1    Venkitaraman, A.R.2    Schilling, K.M.3    Bowen, W.H.4
  • 31
    • 10344249113 scopus 로고    scopus 로고
    • Immobilisation and activity of human α-amylase in the acquired enamel pellicle
    • Hannig C., Attin T., Hannig M., Henze E., Brinkmann K., and Zech R. Immobilisation and activity of human α-amylase in the acquired enamel pellicle. Arch Oral Biol 49 (2004) 469-475
    • (2004) Arch Oral Biol , vol.49 , pp. 469-475
    • Hannig, C.1    Attin, T.2    Hannig, M.3    Henze, E.4    Brinkmann, K.5    Zech, R.6
  • 32
    • 23944476846 scopus 로고    scopus 로고
    • Interactions of Streptococcus mutans glucosyltransferase B with lysozyme in solution and on the surface of hydroxyapatite
    • Kho H.S., Vacca-Smith A.M., Koo H., Scott-Anne K., and Bowen W.H. Interactions of Streptococcus mutans glucosyltransferase B with lysozyme in solution and on the surface of hydroxyapatite. Caries Res 39 (2005) 411-416
    • (2005) Caries Res , vol.39 , pp. 411-416
    • Kho, H.S.1    Vacca-Smith, A.M.2    Koo, H.3    Scott-Anne, K.4    Bowen, W.H.5
  • 33
    • 0019314546 scopus 로고
    • Immunochemical identification and determination of proline-rich proteins in salivary secretions, enamel pellicle, and glandular tissue specimens
    • Kousvelari E.E., Baratz R.S., Burke B., and Oppenheim F.G. Immunochemical identification and determination of proline-rich proteins in salivary secretions, enamel pellicle, and glandular tissue specimens. J Dent Res 59 (1980) 1430-1438
    • (1980) J Dent Res , vol.59 , pp. 1430-1438
    • Kousvelari, E.E.1    Baratz, R.S.2    Burke, B.3    Oppenheim, F.G.4
  • 34
    • 0019797848 scopus 로고
    • Immobilized lactoperoxidase as a biologically active and stable form of an antimicrobial enzyme
    • Tenovuo J., and Kurkijärvi K. Immobilized lactoperoxidase as a biologically active and stable form of an antimicrobial enzyme. Arch Oral Biol 26 (1981) 309-314
    • (1981) Arch Oral Biol , vol.26 , pp. 309-314
    • Tenovuo, J.1    Kurkijärvi, K.2
  • 35
    • 84985817814 scopus 로고
    • Identification of IgA, IgG, lysozyme, albumin, α-amylase and glucosyltransferase in the protein layer adsorbed to hydroxyapatite from whole saliva
    • Rölla G., Ciardi J.E., and Bowen W.H. Identification of IgA, IgG, lysozyme, albumin, α-amylase and glucosyltransferase in the protein layer adsorbed to hydroxyapatite from whole saliva. Scand J Dent Res 91 (1983) 186-190
    • (1983) Scand J Dent Res , vol.91 , pp. 186-190
    • Rölla, G.1    Ciardi, J.E.2    Bowen, W.H.3
  • 36
    • 0024789499 scopus 로고
    • Characterization of in vivo salivary-derived enamel pellicle
    • Al-Hashimi I., and Levine M.J. Characterization of in vivo salivary-derived enamel pellicle. Arch Oral Biol 34 (1989) 289-295
    • (1989) Arch Oral Biol , vol.34 , pp. 289-295
    • Al-Hashimi, I.1    Levine, M.J.2
  • 37
    • 0014103814 scopus 로고
    • The adsorption of human salivary proteins and porcine submaxillary mucin by hydroxyapatite
    • McGaughey C., and Stowell E.C. The adsorption of human salivary proteins and porcine submaxillary mucin by hydroxyapatite. Arch Oral Biol 12 (1967) 815-828
    • (1967) Arch Oral Biol , vol.12 , pp. 815-828
    • McGaughey, C.1    Stowell, E.C.2
  • 38
    • 17544399630 scopus 로고
    • Adsorption of human salivary mucins to hydroxyapatite
    • Tabak L.A., Levine M.J., Jain N.K., et al. Adsorption of human salivary mucins to hydroxyapatite. Arch Oral Biol 30 (1985) 423-427
    • (1985) Arch Oral Biol , vol.30 , pp. 423-427
    • Tabak, L.A.1    Levine, M.J.2    Jain, N.K.3
  • 39
    • 0023026167 scopus 로고
    • Potential role of lysozyme in bactericidal activity of in vitro-acquired salivary pellicle against Streptococcus faecium 9790
    • Germaine G.R., and Tellefson L.M. Potential role of lysozyme in bactericidal activity of in vitro-acquired salivary pellicle against Streptococcus faecium 9790. Infect Immun 54 (1986) 846-854
    • (1986) Infect Immun , vol.54 , pp. 846-854
    • Germaine, G.R.1    Tellefson, L.M.2
  • 40
    • 0028723423 scopus 로고
    • Lysozyme and lactoperoxidase inhibit the adherence of Streptococcus mutans NCTC 10449 (serotype c) to saliva-treated hydroxyapatite in vitro
    • Roger V., Tenovuo J., Lenander-Lumikari M., Soderling E., and Vilja P. Lysozyme and lactoperoxidase inhibit the adherence of Streptococcus mutans NCTC 10449 (serotype c) to saliva-treated hydroxyapatite in vitro. Caries Res 28 (1994) 421-428
    • (1994) Caries Res , vol.28 , pp. 421-428
    • Roger, V.1    Tenovuo, J.2    Lenander-Lumikari, M.3    Soderling, E.4    Vilja, P.5
  • 41
    • 0003049889 scopus 로고
    • Salivary secretion rate, buffer capacity, and pH
    • Tenovuo J.O. (Ed), CRC Press Inc., Boca Raton
    • Birkhed D., and Heintze U. Salivary secretion rate, buffer capacity, and pH. In: Tenovuo J.O. (Ed). Human saliva: clinical chemistry and microbiology vol. I (1989), CRC Press Inc., Boca Raton 25-73
    • (1989) Human saliva: clinical chemistry and microbiology , vol.I , pp. 25-73
    • Birkhed, D.1    Heintze, U.2
  • 42
    • 0000222201 scopus 로고
    • A method of submaxillary saliva collection without cannulization
    • Block P.L., and Brottman S. A method of submaxillary saliva collection without cannulization. N Y State Dent J 28 (1962) 116-118
    • (1962) N Y State Dent J , vol.28 , pp. 116-118
    • Block, P.L.1    Brottman, S.2
  • 43
    • 0017944797 scopus 로고
    • Comparative estimates of bacterial affinities and adsorption sites on hydroxyapatite surfaces
    • Clark W.B., Bammann L.L., and Gibbons R.J. Comparative estimates of bacterial affinities and adsorption sites on hydroxyapatite surfaces. Infect Immun 19 (1978) 846-853
    • (1978) Infect Immun , vol.19 , pp. 846-853
    • Clark, W.B.1    Bammann, L.L.2    Gibbons, R.J.3
  • 44
    • 0014410272 scopus 로고
    • Amino acid analysis: aqueous dimethyl sulfoxide as solvent for the ninhydrin reaction
    • Moore S. Amino acid analysis: aqueous dimethyl sulfoxide as solvent for the ninhydrin reaction. J Biol Chem 243 (1968) 6281-6283
    • (1968) J Biol Chem , vol.243 , pp. 6281-6283
    • Moore, S.1
  • 45
    • 0020669408 scopus 로고
    • Methods for determination of lysozyme activity
    • Grossowicz N., and Ariel M. Methods for determination of lysozyme activity. Methods Biochem Anal 29 (1983) 435-446
    • (1983) Methods Biochem Anal , vol.29 , pp. 435-446
    • Grossowicz, N.1    Ariel, M.2
  • 46
    • 0015912728 scopus 로고
    • The occurrence of repetitive glycopeptide sequences in bovine submaxillary glycoprotein
    • Pigman W., Moschera J., Weis M., and Tettamanti G. The occurrence of repetitive glycopeptide sequences in bovine submaxillary glycoprotein. Eur J Biochem 32 (1973) 148-154
    • (1973) Eur J Biochem , vol.32 , pp. 148-154
    • Pigman, W.1    Moschera, J.2    Weis, M.3    Tettamanti, G.4
  • 47
    • 0026018131 scopus 로고
    • Large-scale purification and characterization of the major phosphoproteins and mucins of human submandibular-sublingual saliva
    • Ramasubbu N., Reddy M.S., Bergey E.J., Haraszthy G.G., Soni S., and Levine M.J. Large-scale purification and characterization of the major phosphoproteins and mucins of human submandibular-sublingual saliva. Biochem J 280 (1991) 341-352
    • (1991) Biochem J , vol.280 , pp. 341-352
    • Ramasubbu, N.1    Reddy, M.S.2    Bergey, E.J.3    Haraszthy, G.G.4    Soni, S.5    Levine, M.J.6
  • 48
    • 0025000513 scopus 로고
    • Lipid binding to gastric mucin: protective effect against oxygen radicals
    • Gong D., Turner B., Bhaskar K.R., and Lamont J.T. Lipid binding to gastric mucin: protective effect against oxygen radicals. Am J Physiol 259 (1990) G681-G686
    • (1990) Am J Physiol , vol.259
    • Gong, D.1    Turner, B.2    Bhaskar, K.R.3    Lamont, J.T.4
  • 49
    • 0026321416 scopus 로고
    • Profound increase in viscosity and aggregation of pig gastric mucin at low pH
    • Bhaskar K.R., Gong D., Bansil R., et al. Profound increase in viscosity and aggregation of pig gastric mucin at low pH. Am J Physiol 261 (1991) G827-G832
    • (1991) Am J Physiol , vol.261
    • Bhaskar, K.R.1    Gong, D.2    Bansil, R.3
  • 50
    • 0031613975 scopus 로고    scopus 로고
    • Composition of pellicles formed in vivo on tooth surfaces in different parts of the dentition, and in vitro on hydroxyapatite
    • Carlen A., Börjesson A.C., Nikdel K., and Olsson J. Composition of pellicles formed in vivo on tooth surfaces in different parts of the dentition, and in vitro on hydroxyapatite. Caries Res 32 (1998) 447-455
    • (1998) Caries Res , vol.32 , pp. 447-455
    • Carlen, A.1    Börjesson, A.C.2    Nikdel, K.3    Olsson, J.4
  • 51
    • 0035118520 scopus 로고    scopus 로고
    • Compositional analysis of human acquired pellicle by mass spectrometry
    • Yao Y., Grogan J., Zehnder M., et al. Compositional analysis of human acquired pellicle by mass spectrometry. Arch Oral Biol 46 (2001) 293-303
    • (2001) Arch Oral Biol , vol.46 , pp. 293-303
    • Yao, Y.1    Grogan, J.2    Zehnder, M.3
  • 52
    • 0036886087 scopus 로고    scopus 로고
    • Influence of dentifrices and dietary components in saliva on wettability of pellicle-coated enamel on vitro and in vivo
    • van der Mei H.C., White D.J., Kamminga-Rasker H.J., et al. Influence of dentifrices and dietary components in saliva on wettability of pellicle-coated enamel on vitro and in vivo. Eur J Oral Sci 110 (2002) 434-438
    • (2002) Eur J Oral Sci , vol.110 , pp. 434-438
    • van der Mei, H.C.1    White, D.J.2    Kamminga-Rasker, H.J.3
  • 53
    • 0028631078 scopus 로고
    • Saliva-bacterium interactions in oral microbial ecology
    • Scannapieco F.A. Saliva-bacterium interactions in oral microbial ecology. Crit Rev Oral Biol Med 5 (1994) 102-119
    • (1994) Crit Rev Oral Biol Med , vol.5 , pp. 102-119
    • Scannapieco, F.A.1
  • 54
    • 0018527869 scopus 로고
    • Kinetics of acetylcholinesterase immobilized on polyethylene tubing
    • Ngo T.T., Laidler K.J., and Yam C.F. Kinetics of acetylcholinesterase immobilized on polyethylene tubing. Can J Biochem 57 (1979) 1200-1203
    • (1979) Can J Biochem , vol.57 , pp. 1200-1203
    • Ngo, T.T.1    Laidler, K.J.2    Yam, C.F.3
  • 55
    • 0024838510 scopus 로고
    • A transmission electron microscopy study of the adsorption patterns of early developing artificial pellicles on human enamel
    • Busscher H.J., Uyen H.M., Stokroos I., and Jongebloed W.L. A transmission electron microscopy study of the adsorption patterns of early developing artificial pellicles on human enamel. Arch Oral Biol 34 (1989) 803-810
    • (1989) Arch Oral Biol , vol.34 , pp. 803-810
    • Busscher, H.J.1    Uyen, H.M.2    Stokroos, I.3    Jongebloed, W.L.4
  • 56
    • 0031242433 scopus 로고    scopus 로고
    • Transmission electron microscopic study of in vivo pellicle formation of dental restorative materials
    • Hannig M. Transmission electron microscopic study of in vivo pellicle formation of dental restorative materials. Eur J Oral Sci 105 (1997) 422-433
    • (1997) Eur J Oral Sci , vol.105 , pp. 422-433
    • Hannig, M.1
  • 57
    • 0033139583 scopus 로고    scopus 로고
    • Ultrastructural investigation of pellicle morphogenesis at two different intraoral sites during 24-h period
    • Hannig M. Ultrastructural investigation of pellicle morphogenesis at two different intraoral sites during 24-h period. Clin Oral Investig 3 (1999) 88-95
    • (1999) Clin Oral Investig , vol.3 , pp. 88-95
    • Hannig, M.1
  • 58
    • 20444476766 scopus 로고    scopus 로고
    • Lysozyme activity in the initially formed in situ pellicle
    • Hannig C., Hoch J., Becker K., Hannig M., and Attin T. Lysozyme activity in the initially formed in situ pellicle. Arch Oral Biol 50 (2005) 821-828
    • (2005) Arch Oral Biol , vol.50 , pp. 821-828
    • Hannig, C.1    Hoch, J.2    Becker, K.3    Hannig, M.4    Attin, T.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.