메뉴 건너뛰기




Volumn 89, Issue 8, 2006, Pages 2911-2918

Expression and bioactivity of recombinant human lysozyme in the milk of transgenic mice

Author keywords

Antibacterial activity; Human lysozyme; Transgenic mice; Whey

Indexed keywords

BOS TAURUS; MAMMALIA; MUS MUSCULUS;

EID: 33746875211     PISSN: 00220302     EISSN: None     Source Type: Journal    
DOI: 10.3168/jds.S0022-0302(06)72563-2     Document Type: Article
Times cited : (42)

References (32)
  • 3
    • 0013852789 scopus 로고
    • Purification and some properties of bovine milk lysozyme
    • Chandan, R. C., R. M. Parry, and K. M. Shahani. 1965. Purification and some properties of bovine milk lysozyme. Biochim. Biophys. Acta 110:389-398.
    • (1965) Biochim. Biophys. Acta , vol.110 , pp. 389-398
    • Chandan, R.C.1    Parry, R.M.2    Shahani, K.M.3
  • 4
    • 0003153739 scopus 로고
    • Lysozyme content of human milk
    • Chandan, R. C., K. M. Shahani, and R. G. Holly. 1964. Lysozyme content of human milk. Nature 204:76-77.
    • (1964) Nature , vol.204 , pp. 76-77
    • Chandan, R.C.1    Shahani, K.M.2    Holly, R.G.3
  • 6
    • 0027523180 scopus 로고
    • Titration of protein transport activity by incremental changes in signal peptide hydrophobicity
    • Doud, S. K., M. M. Chou, and D. A. Kendall. 1993. Titration of protein transport activity by incremental changes in signal peptide hydrophobicity. Biochemistry 32:1251-1256.
    • (1993) Biochemistry , vol.32 , pp. 1251-1256
    • Doud, S.K.1    Chou, M.M.2    Kendall, D.A.3
  • 7
    • 0030455418 scopus 로고    scopus 로고
    • Purification and characterization of lactoferrin, lactoperoxidase, lysozyme and immunoglobulins from camel's milk
    • Elagamy, E. I., R. Ruppanner, A. Ismail, C. P. Champagne, and R. Assaf. 1996. Purification and characterization of lactoferrin, lactoperoxidase, lysozyme and immunoglobulins from camel's milk. Int. Dairy J. 6:129-145.
    • (1996) Int. Dairy J. , vol.6 , pp. 129-145
    • Elagamy, E.I.1    Ruppanner, R.2    Ismail, A.3    Champagne, C.P.4    Assaf, R.5
  • 8
    • 0006007020 scopus 로고
    • G. G. Birch and K. J. Parker, ed. Applied Science Publishers, London, UK
    • Francis, D. 1980. Infant Nutrition. G. G. Birch and K. J. Parker, ed. Applied Science Publishers, London, UK.
    • (1980) Infant Nutrition
    • Francis, D.1
  • 9
    • 0000133661 scopus 로고
    • Defence agents
    • R. G. Jenson, ed. Academic Press, San Diego, CA
    • Goldman, A. S., and R. M. Goldblum. 1995. Defence agents. Pages 727-748 in Handbook of Milk Composition. R. G. Jenson, ed. Academic Press, San Diego, CA.
    • (1995) Handbook of Milk Composition , pp. 727-748
    • Goldman, A.S.1    Goldblum, R.M.2
  • 10
    • 0018700929 scopus 로고
    • Specificity of bacteriolytic enzyme II from a soil amoeba, Hartmannella glebae
    • Hemelt, D. M., B. Mares, and J. M. Upadhyay. 1979. Specificity of bacteriolytic enzyme II from a soil amoeba, Hartmannella glebae. Appl. Environ. Microbiol. 38:373-378.
    • (1979) Appl. Environ. Microbiol. , vol.38 , pp. 373-378
    • Hemelt, D.M.1    Mares, B.2    Upadhyay, J.M.3
  • 13
    • 77956935682 scopus 로고
    • Vertebrate lysozyme
    • P. D. Boyer, ed. Academic Press, New York, NY
    • Imoto, T., L. N. Johnson, A. T. C. North, D. C. Philips, and J. A. Rupley. 1972. Vertebrate lysozyme. Pages 665-868 in The Enzyme. Vol. 7. P. D. Boyer, ed. Academic Press, New York, NY.
    • (1972) The Enzyme , vol.7 , pp. 665-868
    • Imoto, T.1    Johnson, L.N.2    North, A.T.C.3    Philips, D.C.4    Rupley, J.A.5
  • 14
    • 0029147016 scopus 로고
    • Physical and conformational properties of synthetic idealized signal sequences parallel their biological function
    • Izard, J. W., M. B. Doughty, and D. A. Kendall. 1995. Physical and conformational properties of synthetic idealized signal sequences parallel their biological function. Biochemistry 34:9904-9912.
    • (1995) Biochemistry , vol.34 , pp. 9904-9912
    • Izard, J.W.1    Doughty, M.B.2    Kendall, D.A.3
  • 15
    • 0016517114 scopus 로고
    • Heat stability and reactivation of mare milk lysozyme
    • Jauregui-Adell, J. 1975. Heat stability and reactivation of mare milk lysozyme. J. Dairy Sci. 58:835-838.
    • (1975) J. Dairy Sci. , vol.58 , pp. 835-838
    • Jauregui-Adell, J.1
  • 17
    • 3042808093 scopus 로고    scopus 로고
    • Variable expression of human lactoferrin gene in mice milk driven by its 90 KB upstream flanking sequences
    • Liu, Z., C. Zhao, B. Fan, Y. Dai, L. Wang, M. Zheng, J. Feng, Y. Chen, Y. Duan, and N. Li. 2004. Variable expression of human lactoferrin gene in mice milk driven by its 90 KB upstream flanking sequences. Anim. Biotechnol. 15:21-31.
    • (2004) Anim. Biotechnol. , vol.15 , pp. 21-31
    • Liu, Z.1    Zhao, C.2    Fan, B.3    Dai, Y.4    Wang, L.5    Zheng, M.6    Feng, J.7    Chen, Y.8    Duan, Y.9    Li, N.10
  • 18
    • 0022371729 scopus 로고
    • Biochemistry and physiological function of human milk proteins
    • Lönnerdal, B. 1985. Biochemistry and physiological function of human milk proteins. Am. J. Clin. Nutr. 42:1299-1317.
    • (1985) Am. J. Clin. Nutr. , vol.42 , pp. 1299-1317
    • Lönnerdal, B.1
  • 19
    • 0029440746 scopus 로고
    • The effect of mammary gland expression of human lysozyme on the properties of milk from transgenic mice
    • Maga, E. A., and G. B. Anderson. 1995. The effect of mammary gland expression of human lysozyme on the properties of milk from transgenic mice. J. Dairy Sci. 78:2645-2652.
    • (1995) J. Dairy Sci. , vol.78 , pp. 2645-2652
    • Maga, E.A.1    Anderson, G.B.2
  • 20
    • 0028066197 scopus 로고
    • Expression of human lysozyme mRNA in the mammary gland of transgenic mice
    • Maga, E., G. Anderson, M. Huang, and J. Murray. 1994. Expression of human lysozyme mRNA in the mammary gland of transgenic mice. Transgenic Res. 3:36-42.
    • (1994) Transgenic Res. , vol.3 , pp. 36-42
    • Maga, E.1    Anderson, G.2    Huang, M.3    Murray, J.4
  • 21
    • 0022552217 scopus 로고
    • Determination of lysozyme activity at low levels with emphasis on the milk enzyme
    • McKenzie, H. A., and F. H. White, Jr. 1986. Determination of lysozyme activity at low levels with emphasis on the milk enzyme. Anal. Biochem. 157:367-374.
    • (1986) Anal. Biochem. , vol.157 , pp. 367-374
    • McKenzie, H.A.1    White Jr., F.H.2
  • 22
    • 0033402852 scopus 로고    scopus 로고
    • Protein purification and gene isolation of chlamysin, a cold-active lysozyme-like enzyme with antibacterial activity
    • Nilsen, I. W., K. Overbo, E. Sandsdalen, E. Sandaker, K. Sletten, and B. Myrnes. 1999. Protein purification and gene isolation of chlamysin, a cold-active lysozyme-like enzyme with antibacterial activity. FEBS Lett. 464:153-158.
    • (1999) FEBS Lett. , vol.464 , pp. 153-158
    • Nilsen, I.W.1    Overbo, K.2    Sandsdalen, E.3    Sandaker, E.4    Sletten, K.5    Myrnes, B.6
  • 23
    • 0037278025 scopus 로고    scopus 로고
    • Solution structure and activity of mouse lysozyme M
    • Obita, T., T. Ueda, and T. Imoto. 2003. Solution structure and activity of mouse lysozyme M. Cell Mol. Life Sci. 60:176-184.
    • (2003) Cell Mol. Life Sci. , vol.60 , pp. 176-184
    • Obita, T.1    Ueda, T.2    Imoto, T.3
  • 26
    • 0028859402 scopus 로고
    • High-level, stage- and mammary-tissue-specific expression of a caprine κ-casein-encoding minigene driven by a β-casein promoter in transgenic mice
    • Persuy, M. A., S. Legrain, C. Printz, M. G. Stinnakre, L. Lepourry, G. Brignon, and J. C. Mercier. 1995. High-level, stage- and mammary-tissue-specific expression of a caprine κ-casein-encoding minigene driven by a β-casein promoter in transgenic mice. Gene 165:291-296.
    • (1995) Gene , vol.165 , pp. 291-296
    • Persuy, M.A.1    Legrain, S.2    Printz, C.3    Stinnakre, M.G.4    Lepourry, L.5    Brignon, G.6    Mercier, J.C.7
  • 27
    • 0034773690 scopus 로고    scopus 로고
    • A new β-lactoglobulin-based vector targets luciferase cDNA expression to the mammary gland of transgenic mice
    • Reichenstein, M., H. Gottlieb, G. M. Damari, E. Iavnilovitch, and I. Barash. 2001. A new β-lactoglobulin-based vector targets luciferase cDNA expression to the mammary gland of transgenic mice. Transgenic Res. 10:445-456.
    • (2001) Transgenic Res. , vol.10 , pp. 445-456
    • Reichenstein, M.1    Gottlieb, H.2    Damari, G.M.3    Iavnilovitch, E.4    Barash, I.5
  • 28
    • 0026441239 scopus 로고
    • Cloning of the goat β-casein-encoding gene and expression in transgenic mice
    • Roberts, B., P. DiTullio, J. Vitale, K. Hehir, and K. Gordon. 1992. Cloning of the goat β-casein-encoding gene and expression in transgenic mice. Gene 121:255-262.
    • (1992) Gene , vol.121 , pp. 255-262
    • Roberts, B.1    DiTullio, P.2    Vitale, J.3    Hehir, K.4    Gordon, K.5
  • 29
    • 34247124903 scopus 로고
    • Measure of lysozyme activity and the ultraviolet inactivation of lysozyme
    • Shugar, D. 1952. Measure of lysozyme activity and the ultraviolet inactivation of lysozyme. Biochim. Biophys. Acta 8:302.
    • (1952) Biochim. Biophys. Acta , vol.8 , pp. 302
    • Shugar, D.1
  • 30
    • 0028783889 scopus 로고
    • Rabbit whey acidic protein gene upstream region controls high-level expression of bovine growth hormone in the mammary gland of transgenic mice
    • Thepot, D., E. Devinoy, M. L. Fontaine, M. G. Stinnakre, M. Massoud, G. Kann, and L. M. Houdebine. 1995. Rabbit whey acidic protein gene upstream region controls high-level expression of bovine growth hormone in the mammary gland of transgenic mice. Mol. Reprod. Dev. 42:261-267.
    • (1995) Mol. Reprod. Dev. , vol.42 , pp. 261-267
    • Thepot, D.1    Devinoy, E.2    Fontaine, M.L.3    Stinnakre, M.G.4    Massoud, M.5    Kann, G.6    Houdebine, L.M.7
  • 32
    • 0037258101 scopus 로고    scopus 로고
    • Influence of signal peptide sequences on the expression of heterogeneous proteins in Pichia pastoris
    • Xiong, A., R. Peng, X. Li, H. Fan, Q. Yao, M. Guo, and S. Zhang. 2003. Influence of signal peptide sequences on the expression of heterogeneous proteins in Pichia pastoris. Acta Biochim. Biophys. Sin. 35:154-160.
    • (2003) Acta Biochim. Biophys. Sin. , vol.35 , pp. 154-160
    • Xiong, A.1    Peng, R.2    Li, X.3    Fan, H.4    Yao, Q.5    Guo, M.6    Zhang, S.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.