메뉴 건너뛰기




Volumn 6, Issue 3, 2011, Pages

Characterization of bioactive recombinant human lysozyme expressed in milk of cloned transgenic cattle

Author keywords

[No Author keywords available]

Indexed keywords

FAT; LACTOSE; LYSOZYME; PROTEIN; RECOMBINANT HUMAN LYSOZYME; UNCLASSIFIED DRUG; HEN EGG LYSOZYME; RECOMBINANT PROTEIN;

EID: 79952775522     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0017593     Document Type: Article
Times cited : (122)

References (58)
  • 1
    • 0000646464 scopus 로고
    • On a remarkable bacteriolytic element found in tissues and secretions
    • Fleming A, (1922) On a remarkable bacteriolytic element found in tissues and secretions. Proc Roy Soc Ser B93: 306-317.
    • (1922) Proc Roy Soc Ser , vol.B93 , pp. 306-317
    • Fleming, A.1
  • 2
    • 0021490172 scopus 로고
    • What's new in lysozyme research? Always a model system, today as yesterday
    • Jolles P, Jolles J, (1984) What's new in lysozyme research? Always a model system, today as yesterday. Mol Cell Biochem 63: 165-189.
    • (1984) Mol Cell Biochem , vol.63 , pp. 165-189
    • Jolles, P.1    Jolles, J.2
  • 3
    • 0031056829 scopus 로고    scopus 로고
    • Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis
    • Booth DR, Sunde M, Bellotti V, Robinson CV, Hutchinson WL, et al. (1997) Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis. Nature 385: 787-793.
    • (1997) Nature , vol.385 , pp. 787-793
    • Booth, D.R.1    Sunde, M.2    Bellotti, V.3    Robinson, C.V.4    Hutchinson, W.L.5
  • 5
    • 0016664344 scopus 로고
    • The distribution of muramidase (lysozyme) in human tissues
    • Mason DY, Taylor CR, (1975) The distribution of muramidase (lysozyme) in human tissues. J Clin Pathol 28: 124-132.
    • (1975) J Clin Pathol , vol.28 , pp. 124-132
    • Mason, D.Y.1    Taylor, C.R.2
  • 7
    • 0031774839 scopus 로고    scopus 로고
    • A novel anti-inflammatory activity of lysozyme: modulation of serum complement activation
    • Ogundele MO, (1998) A novel anti-inflammatory activity of lysozyme: modulation of serum complement activation. Mediators Inflamm 7: 363-365.
    • (1998) Mediators Inflamm , vol.7 , pp. 363-365
    • Ogundele, M.O.1
  • 8
    • 15444380147 scopus 로고    scopus 로고
    • Structural and functional modeling of human lysozyme reveals a unique nonapeptide, HL9, with anti-HIV activity
    • Lee-Huang S, Maiorov V, Huang PL, Ng A, Lee HC, et al. (2005) Structural and functional modeling of human lysozyme reveals a unique nonapeptide, HL9, with anti-HIV activity. Biochemistry 44: 4648-4655.
    • (2005) Biochemistry , vol.44 , pp. 4648-4655
    • Lee-Huang, S.1    Maiorov, V.2    Huang, P.L.3    Ng, A.4    Lee, H.C.5
  • 9
    • 0030730493 scopus 로고    scopus 로고
    • The antifungal effect of lactoferrin and lysozyme on Candida krusei and Candida albicans
    • Samaranayake YH, Samaranayake LP, Wu PC, So M, (1997) The antifungal effect of lactoferrin and lysozyme on Candida krusei and Candida albicans. Apmis 105: 875-883.
    • (1997) Apmis , vol.105 , pp. 875-883
    • Samaranayake, Y.H.1    Samaranayake, L.P.2    Wu, P.C.3    So, M.4
  • 10
    • 0018171622 scopus 로고
    • Radioimmunoassay for urinary lysozyme in human serum from leukemic patients
    • Peeters TL, Depraetere YR, Vantrappen GR, (1978) Radioimmunoassay for urinary lysozyme in human serum from leukemic patients. Clin Chem 24: 2155-2157.
    • (1978) Clin Chem , vol.24 , pp. 2155-2157
    • Peeters, T.L.1    Depraetere, Y.R.2    Vantrappen, G.R.3
  • 11
    • 33644925290 scopus 로고    scopus 로고
    • Hen egg white lysozyme as an inhibitor of mushroom tyrosinase
    • Li B, Huang Y, Paskewitz SM, (2006) Hen egg white lysozyme as an inhibitor of mushroom tyrosinase. FEBS Lett 580: 1877-1882.
    • (2006) FEBS Lett , vol.580 , pp. 1877-1882
    • Li, B.1    Huang, Y.2    Paskewitz, S.M.3
  • 12
    • 34548827034 scopus 로고    scopus 로고
    • Designer milk
    • Sabikhi L, (2007) Designer milk. Adv Food Nutr Res 53: 161-198.
    • (2007) Adv Food Nutr Res , vol.53 , pp. 161-198
    • Sabikhi, L.1
  • 13
    • 0023728756 scopus 로고
    • The chemistry of lysozyme and its use as a food preservative and a pharmaceutical
    • Proctor VA, Cunningham FE, (1988) The chemistry of lysozyme and its use as a food preservative and a pharmaceutical. Crit Rev Food Sci Nutr 26: 359-395.
    • (1988) Crit Rev Food Sci Nutr , vol.26 , pp. 359-395
    • Proctor, V.A.1    Cunningham, F.E.2
  • 14
    • 0031843536 scopus 로고    scopus 로고
    • Immunonutrition: the pediatric experience
    • Levy J, (1998) Immunonutrition: the pediatric experience. Nutrition 14: 641-647.
    • (1998) Nutrition , vol.14 , pp. 641-647
    • Levy, J.1
  • 15
    • 0037901694 scopus 로고    scopus 로고
    • Nutritional and physiologic significance of human milk proteins
    • Lonnerdal B, (2003) Nutritional and physiologic significance of human milk proteins. Am J Clin Nutr 77: 1537S-1543S.
    • (2003) Am J Clin Nutr , vol.77
    • Lonnerdal, B.1
  • 17
    • 0035703976 scopus 로고    scopus 로고
    • Changes in lactoferrin and lysozyme levels in human milk during the first twelve weeks of lactation
    • Montagne P, Cuilliere ML, Mole C, Bene MC, Faure G, (2001) Changes in lactoferrin and lysozyme levels in human milk during the first twelve weeks of lactation. Adv Exp Med Biol 501: 241-247.
    • (2001) Adv Exp Med Biol , vol.501 , pp. 241-247
    • Montagne, P.1    Cuilliere, M.L.2    Mole, C.3    Bene, M.C.4    Faure, G.5
  • 18
    • 24944449486 scopus 로고    scopus 로고
    • Comparison of blood and milk non-specific immune parameters in heifers after calving in relation to udder health
    • Piccinini R, Binda E, Belotti M, Casirani G, Zecconi A, (2005) Comparison of blood and milk non-specific immune parameters in heifers after calving in relation to udder health. Vet Res 36: 747-757.
    • (2005) Vet Res , vol.36 , pp. 747-757
    • Piccinini, R.1    Binda, E.2    Belotti, M.3    Casirani, G.4    Zecconi, A.5
  • 19
    • 0027252943 scopus 로고
    • The primary structures and properties of non-stomach lysozymes of sheep and cow, and implication for functional divergence of lysozyme
    • Ito Y, Yamada H, Nakamura M, Yoshikawa A, Ueda T, et al. (1993) The primary structures and properties of non-stomach lysozymes of sheep and cow, and implication for functional divergence of lysozyme. Eur J Biochem 213: 649-658.
    • (1993) Eur J Biochem , vol.213 , pp. 649-658
    • Ito, Y.1    Yamada, H.2    Nakamura, M.3    Yoshikawa, A.4    Ueda, T.5
  • 20
    • 58149311483 scopus 로고    scopus 로고
    • Secreted expression of human lysozyme in the yeast Pichia pastoris under the direction of the signal peptide from human serum albumin
    • Xiong R, Chen J, (2008) Secreted expression of human lysozyme in the yeast Pichia pastoris under the direction of the signal peptide from human serum albumin. Biotechnol Appl Biochem 51: 129-134.
    • (2008) Biotechnol Appl Biochem , vol.51 , pp. 129-134
    • Xiong, R.1    Chen, J.2
  • 21
    • 65249146586 scopus 로고    scopus 로고
    • Enhanced Human Lysozyme Production by Kluyveromyces lactis
    • Demirci1 ELHaA
    • Demirci1 ELHaA, (2009) Enhanced Human Lysozyme Production by Kluyveromyces lactis. Food and Bioprocess Technology 2: 222-228.
    • (2009) Food and Bioprocess Technology , vol.2 , pp. 222-228
  • 22
    • 0035988816 scopus 로고    scopus 로고
    • Expression of functional recombinant human lysozyme in transgenic rice cell culture
    • Huang J, Wu L, Yalda D, Adkins Y, Kelleher SL, et al. (2002) Expression of functional recombinant human lysozyme in transgenic rice cell culture. Transgenic Res 11: 229-239.
    • (2002) Transgenic Res , vol.11 , pp. 229-239
    • Huang, J.1    Wu, L.2    Yalda, D.3    Adkins, Y.4    Kelleher, S.L.5
  • 23
    • 58849122869 scopus 로고    scopus 로고
    • Production of pharmaceutical proteins by transgenic animals
    • Houdebine LM, (2009) Production of pharmaceutical proteins by transgenic animals. Comp Immunol Microbiol Infect Dis 32: 107-121.
    • (2009) Comp Immunol Microbiol Infect Dis , vol.32 , pp. 107-121
    • Houdebine, L.M.1
  • 24
    • 0032105836 scopus 로고    scopus 로고
    • The mammary gland as a bioreactor: expression, processing, and production of recombinant proteins
    • Clark AJ, (1998) The mammary gland as a bioreactor: expression, processing, and production of recombinant proteins. J Mammary Gland Biol Neoplasia 3: 337-350.
    • (1998) J Mammary Gland Biol Neoplasia , vol.3 , pp. 337-350
    • Clark, A.J.1
  • 25
    • 33846244198 scopus 로고    scopus 로고
    • Human lysozyme expressed in the mammary gland of transgenic dairy goats can inhibit the growth of bacteria that cause mastitis and the cold-spoilage of milk
    • Maga EA, Cullor JS, Smith W, Anderson GB, Murray JD, (2006) Human lysozyme expressed in the mammary gland of transgenic dairy goats can inhibit the growth of bacteria that cause mastitis and the cold-spoilage of milk. Foodborne Pathog Dis 3: 384-392.
    • (2006) Foodborne Pathog Dis , vol.3 , pp. 384-392
    • Maga, E.A.1    Cullor, J.S.2    Smith, W.3    Anderson, G.B.4    Murray, J.D.5
  • 26
    • 0029440746 scopus 로고
    • The effect of mammary gland expression of human lysozyme on the properties of milk from transgenic mice
    • Maga EA, Anderson GB, Murray JD, (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    Murray, J.D.3
  • 27
    • 32444436672 scopus 로고    scopus 로고
    • Production and processing of milk from transgenic goats expressing human lysozyme in the mammary gland
    • Maga EA, Shoemaker CF, Rowe JD, Bondurant RH, Anderson GB, et al. (2006) Production and processing of milk from transgenic goats expressing human lysozyme in the mammary gland. J Dairy Sci 89: 518-524.
    • (2006) J Dairy Sci , vol.89 , pp. 518-524
    • Maga, E.A.1    Shoemaker, C.F.2    Rowe, J.D.3    Bondurant, R.H.4    Anderson, G.B.5
  • 28
    • 33746875211 scopus 로고    scopus 로고
    • Expression and bioactivity of recombinant human lysozyme in the milk of transgenic mice
    • Yu Z, Meng Q, Yu H, Fan B, Yu S, et al. (2006) Expression and bioactivity of recombinant human lysozyme in the milk of transgenic mice. J Dairy Sci 89: 2911-2918.
    • (2006) J Dairy Sci , vol.89 , pp. 2911-2918
    • Yu, Z.1    Meng, Q.2    Yu, H.3    Fan, B.4    Yu, S.5
  • 29
    • 33745052602 scopus 로고    scopus 로고
    • Factors influencing recombinant human lysozyme extraction and cation exchange adsorption
    • Wilken LR, Nikolov ZL, (2006) Factors influencing recombinant human lysozyme extraction and cation exchange adsorption. Biotechnol Prog 22: 745-752.
    • (2006) Biotechnol Prog , vol.22 , pp. 745-752
    • Wilken, L.R.1    Nikolov, Z.L.2
  • 30
    • 23444458486 scopus 로고    scopus 로고
    • Genetically enhanced cows resist intramammary Staphylococcus aureus infection
    • Wall RJ, Powell AM, Paape MJ, Kerr DE, Bannerman DD, et al. (2005) Genetically enhanced cows resist intramammary Staphylococcus aureus infection. Nat Biotechnol 23: 445-451.
    • (2005) Nat Biotechnol , vol.23 , pp. 445-451
    • Wall, R.J.1    Powell, A.M.2    Paape, M.J.3    Kerr, D.E.4    Bannerman, D.D.5
  • 31
    • 0142226586 scopus 로고    scopus 로고
    • Application of transgenesis in livestock for agriculture and biomedicine
    • Niemann H, Kues WA, (2003) Application of transgenesis in livestock for agriculture and biomedicine. Anim Reprod Sci 79: 291-317.
    • (2003) Anim Reprod Sci , vol.79 , pp. 291-317
    • Niemann, H.1    Kues, W.A.2
  • 32
    • 55149093179 scopus 로고    scopus 로고
    • Cattle mammary bioreactor generated by a novel procedure of transgenic cloning for large-scale production of functional human lactoferrin
    • Yang P, Wang J, Gong G, Sun X, Zhang R, et al. (2008) Cattle mammary bioreactor generated by a novel procedure of transgenic cloning for large-scale production of functional human lactoferrin. PLoS One 3: e3453.
    • (2008) PLoS One , vol.3
    • Yang, P.1    Wang, J.2    Gong, G.3    Sun, X.4    Zhang, R.5
  • 33
    • 68949219589 scopus 로고    scopus 로고
    • Transgene expression is associated with copy number and cytomegalovirus promoter methylation in transgenic pigs
    • Kong Q, Wu M, Huan Y, Zhang L, Liu H, et al. (2009) Transgene expression is associated with copy number and cytomegalovirus promoter methylation in transgenic pigs. PLoS One 4: e6679.
    • (2009) PLoS One , vol.4
    • Kong, Q.1    Wu, M.2    Huan, Y.3    Zhang, L.4    Liu, H.5
  • 35
    • 0042871633 scopus 로고    scopus 로고
    • Cloning adult farm animals: a review of the possibilities and problems associated with somatic cell nuclear transfer
    • Edwards JL, Schrick FN, McCracken MD, van Amstel SR, Hopkins FM, et al. (2003) Cloning adult farm animals: a review of the possibilities and problems associated with somatic cell nuclear transfer. Am J Reprod Immunol 50: 113-123.
    • (2003) Am J Reprod Immunol , vol.50 , pp. 113-123
    • Edwards, J.L.1    Schrick, F.N.2    McCracken, M.D.3    van Amstel, S.R.4    Hopkins, F.M.5
  • 36
    • 34249693566 scopus 로고    scopus 로고
    • Quantitative monitoring of pluripotency gene activation after somatic cloning in cattle
    • Wuensch A, Habermann FA, Kurosaka S, Klose R, Zakhartchenko V, et al. (2007) Quantitative monitoring of pluripotency gene activation after somatic cloning in cattle. Biol Reprod 76: 983-991.
    • (2007) Biol Reprod , vol.76 , pp. 983-991
    • Wuensch, A.1    Habermann, F.A.2    Kurosaka, S.3    Klose, R.4    Zakhartchenko, V.5
  • 37
    • 22744456385 scopus 로고    scopus 로고
    • Epigenetic mechanisms affect mutant p53 transgene expression in WAP-mutp53 transgenic mice
    • Krepulat F, Lohler J, Heinlein C, Hermannstadter A, Tolstonog GV, et al. (2005) Epigenetic mechanisms affect mutant p53 transgene expression in WAP-mutp53 transgenic mice. Oncogene 24: 4645-4659.
    • (2005) Oncogene , vol.24 , pp. 4645-4659
    • Krepulat, F.1    Lohler, J.2    Heinlein, C.3    Hermannstadter, A.4    Tolstonog, G.V.5
  • 38
    • 84984498379 scopus 로고
    • Affinity chromatography of human saliva lysozyme and effect of pH and ionic strength on lytic activity
    • Vasstrand EN, Jensen HB, (1980) Affinity chromatography of human saliva lysozyme and effect of pH and ionic strength on lytic activity. Scand J Dent Res 88: 219-228.
    • (1980) Scand J Dent Res , vol.88 , pp. 219-228
    • Vasstrand, E.N.1    Jensen, H.B.2
  • 39
    • 13244277811 scopus 로고    scopus 로고
    • Efficient secretion of human lysozyme from the yeast, Kluyveromyces lactis
    • Iwata T, Tanaka R, Suetsugu M, Ishibashi M, Tokunaga H, et al. (2004) Efficient secretion of human lysozyme from the yeast, Kluyveromyces lactis. Biotechnol Lett 26: 1803-1808.
    • (2004) Biotechnol Lett , vol.26 , pp. 1803-1808
    • Iwata, T.1    Tanaka, R.2    Suetsugu, M.3    Ishibashi, M.4    Tokunaga, H.5
  • 40
    • 67849117184 scopus 로고    scopus 로고
    • Abnormal expression of TIMP-2, SOD, vimentin and PAI proteins in cloned bovine placentae
    • Kim HR, Naruse K, Lee HR, Han RX, Park CS, et al. (2009) Abnormal expression of TIMP-2, SOD, vimentin and PAI proteins in cloned bovine placentae. Reprod Domest Anim 44: 714-717.
    • (2009) Reprod Domest Anim , vol.44 , pp. 714-717
    • Kim, H.R.1    Naruse, K.2    Lee, H.R.3    Han, R.X.4    Park, C.S.5
  • 41
    • 57749115698 scopus 로고    scopus 로고
    • Expression and characterization of bioactive recombinant human alpha-lactalbumin in the milk of transgenic cloned cows
    • Wang J, Yang P, Tang B, Sun X, Zhang R, et al. (2008) Expression and characterization of bioactive recombinant human alpha-lactalbumin in the milk of transgenic cloned cows. J Dairy Sci 91: 4466-4476.
    • (2008) J Dairy Sci , vol.91 , pp. 4466-4476
    • Wang, J.1    Yang, P.2    Tang, B.3    Sun, X.4    Zhang, R.5
  • 42
    • 33845232078 scopus 로고    scopus 로고
    • Compositional analysis of dairy products derived from clones and cloned transgenic cattle
    • Laible G, Brophy B, Knighton D, Wells DN, (2007) Compositional analysis of dairy products derived from clones and cloned transgenic cattle. Theriogenology 67: 166-177.
    • (2007) Theriogenology , vol.67 , pp. 166-177
    • Laible, G.1    Brophy, B.2    Knighton, D.3    Wells, D.N.4
  • 44
    • 79952759804 scopus 로고    scopus 로고
    • AGRICULTURAL QUALITY & STANDARDS-Green food-Milk products China NY/T 657-2007
    • AGRICULTURAL QUALITY & STANDARDS-Green food-Milk products China NY/T 657-2007.
  • 45
    • 78149467972 scopus 로고    scopus 로고
    • Evaluating the fitness of human lysozyme transgenic dairy goats: growth and reproductive traits
    • Jackson KA, Berg JM, Murray JD, Maga EA, (2010) Evaluating the fitness of human lysozyme transgenic dairy goats: growth and reproductive traits. Transgenic Res pp. 977-986.
    • (2010) Transgenic Res , pp. 977-986
    • Jackson, K.A.1    Berg, J.M.2    Murray, J.D.3    Maga, E.A.4
  • 46
    • 33746570234 scopus 로고    scopus 로고
    • Analysis of posttranslational modifications of proteins by tandem mass spectrometry
    • Larsen MR, Trelle MB, Thingholm TE, Jensen ON, (2006) Analysis of posttranslational modifications of proteins by tandem mass spectrometry. Biotechniques 40: 790-798.
    • (2006) Biotechniques , vol.40 , pp. 790-798
    • Larsen, M.R.1    Trelle, M.B.2    Thingholm, T.E.3    Jensen, O.N.4
  • 47
  • 48
    • 70349925445 scopus 로고    scopus 로고
    • High temperature, short time pasteurization temperatures inversely affect bacterial numbers during refrigerated storage of pasteurized fluid milk
    • Ranieri ML, Huck JR, Sonnen M, Barbano DM, Boor KJ, (2009) High temperature, short time pasteurization temperatures inversely affect bacterial numbers during refrigerated storage of pasteurized fluid milk. J Dairy Sci 92: 4823-4832.
    • (2009) J Dairy Sci , vol.92 , pp. 4823-4832
    • Ranieri, M.L.1    Huck, J.R.2    Sonnen, M.3    Barbano, D.M.4    Boor, K.J.5
  • 49
    • 0014687514 scopus 로고
    • The dependence of lysozyme activity on pH and ionic strength
    • Davies RC, Neuberger A, Wilson BM, (1969) The dependence of lysozyme activity on pH and ionic strength. Biochim Biophys Acta 178: 294-305.
    • (1969) Biochim Biophys Acta , vol.178 , pp. 294-305
    • Davies, R.C.1    Neuberger, A.2    Wilson, B.M.3
  • 51
    • 0034869858 scopus 로고    scopus 로고
    • The lysozyme mechanism sorted - after 50 years
    • Kirby AJ, (2001) The lysozyme mechanism sorted - after 50 years. Nat Struct Biol 8: 737-739.
    • (2001) Nat Struct Biol , vol.8 , pp. 737-739
    • Kirby, A.J.1
  • 52
    • 0023944465 scopus 로고
    • Engineering of human lysozyme as a polyelectrolyte by the alteration of molecular surface charge
    • Muraki M, Morikawa M, Jigami Y, Tanaka H, (1988) Engineering of human lysozyme as a polyelectrolyte by the alteration of molecular surface charge. Protein Eng 2: 49-54.
    • (1988) Protein Eng , vol.2 , pp. 49-54
    • Muraki, M.1    Morikawa, M.2    Jigami, Y.3    Tanaka, H.4
  • 53
    • 33644535578 scopus 로고    scopus 로고
    • Comparison of the cariogenicity of cola, honey, cow milk, human milk, and sucrose
    • Bowen WH, Lawrence RA, (2005) Comparison of the cariogenicity of cola, honey, cow milk, human milk, and sucrose. Pediatrics 116: 921-926.
    • (2005) Pediatrics , vol.116 , pp. 921-926
    • Bowen, W.H.1    Lawrence, R.A.2
  • 54
    • 42449129106 scopus 로고    scopus 로고
    • Lysozyme transgenic goats' milk influences gastrointestinal morphology in young pigs
    • Brundige DR, Maga EA, Klasing KC, Murray JD, (2008) Lysozyme transgenic goats' milk influences gastrointestinal morphology in young pigs. J Nutr 138: 921-926.
    • (2008) J Nutr , vol.138 , pp. 921-926
    • Brundige, D.R.1    Maga, E.A.2    Klasing, K.C.3    Murray, J.D.4
  • 55
    • 77954534431 scopus 로고    scopus 로고
    • Consumption of pasteurized human lysozyme transgenic goats' milk alters serum metabolite profile in young pigs
    • Brundige DR, Maga EA, Klasing KC, Murray JD, Consumption of pasteurized human lysozyme transgenic goats' milk alters serum metabolite profile in young pigs. Transgenic Res 19: 563-574.
    • Transgenic Res , vol.19 , pp. 563-574
    • Brundige, D.R.1    Maga, E.A.2    Klasing, K.C.3    Murray, J.D.4
  • 56
    • 4744347342 scopus 로고    scopus 로고
    • Production of transgenic blastocyst by nuclear transfer from different types of somatic cells in cattle
    • Gong G, Dai Y, Fan B, Zhu H, Wang H, et al. (2004) Production of transgenic blastocyst by nuclear transfer from different types of somatic cells in cattle. Sci China C Life Sci 47: 183-189.
    • (2004) Sci China C Life Sci , vol.47 , pp. 183-189
    • Gong, G.1    Dai, Y.2    Fan, B.3    Zhu, H.4    Wang, H.5
  • 57
    • 56749170308 scopus 로고    scopus 로고
    • Heterologous expression and characterization of glycogen branching enzyme from Synechocystis sp. PCC6803
    • Lee BH, Yoo YH, Ryu JH, Kim TJ, Yoo SH, (2008) Heterologous expression and characterization of glycogen branching enzyme from Synechocystis sp. PCC6803. J Microbiol Biotechnol 18: 1386-1392.
    • (2008) J Microbiol Biotechnol , vol.18 , pp. 1386-1392
    • Lee, B.H.1    Yoo, Y.H.2    Ryu, J.H.3    Kim, T.J.4    Yoo, S.H.5
  • 58
    • 34247124903 scopus 로고
    • The measurement of lysozyme activity and the ultra-violet inactivation of lysozyme
    • Shugar D, (1952) The measurement of lysozyme activity and the ultra-violet inactivation of lysozyme. Biochim Biophys Acta 8: 302-309.
    • (1952) Biochim Biophys Acta , vol.8 , pp. 302-309
    • Shugar, D.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.