메뉴 건너뛰기




Volumn 44, Issue 3, 1996, Pages 953-960

Genetic modification of bovine β-casein and its expression in the milk of transgenic mice

Author keywords

Bovine casein; Site directed mutagenesis; Transgenic

Indexed keywords

BOVINAE; MUS MUSCULUS;

EID: 0004026767     PISSN: 00218561     EISSN: None     Source Type: Journal    
DOI: 10.1021/jf950566k     Document Type: Article
Times cited : (5)

References (34)
  • 1
    • 0016382122 scopus 로고
    • Structure of the carbohydrate units of IgE immunoglobulin
    • Baenziger, J.; Kornfeld, S. Structure of the carbohydrate units of IgE immunoglobulin. J. Biol. Chem. 1974, 249, 1897-1903.
    • (1974) J. Biol. Chem. , vol.249 , pp. 1897-1903
    • Baenziger, J.1    Kornfeld, S.2
  • 2
    • 0020713174 scopus 로고
    • Structural requirements of N-glycosylation of proteins
    • Bause, E. Structural requirements of N-glycosylation of proteins. Biochem. J. 1983, 209, 331-336.
    • (1983) Biochem. J. , vol.209 , pp. 331-336
    • Bause, E.1
  • 3
    • 0021256792 scopus 로고
    • Model studies on N-glycosylation of proteins
    • Bause, E. Model studies on N-glycosylation of proteins. Biochem. Soc. Trans. 1984, 12, 514-517.
    • (1984) Biochem. Soc. Trans. , vol.12 , pp. 514-517
    • Bause, E.1
  • 4
    • 0028469708 scopus 로고
    • Variation in expression of a bovine α-lactalbumin transgene in the milk of transgenic mice
    • Bleck, G. T.; Bremel, R. D. Variation in expression of a bovine α-lactalbumin transgene in the milk of transgenic mice. J. Dairy Sci. 1994, 77, 1897-1904.
    • (1994) J. Dairy Sci. , vol.77 , pp. 1897-1904
    • Bleck, G.T.1    Bremel, R.D.2
  • 5
    • 0002696392 scopus 로고
    • Abnormal properties of milk from transgenic mice expressing bovine β-casein under control of the bovine α-lactalbumin 5′ flanking region
    • Bleck, G. T.; Jiménez-Flores, R.; Bremel, R. D. Abnormal properties of milk from transgenic mice expressing bovine β-casein under control of the bovine α-lactalbumin 5′ flanking region. Int. Dairy J. 1995, 5, 619-632.
    • (1995) Int. Dairy J. , vol.5 , pp. 619-632
    • Bleck, G.T.1    Jiménez-Flores, R.2    Bremel, R.D.3
  • 7
    • 0000207162 scopus 로고
    • Solubility and emulsifying properties of caseins modified enzymatically by Staphylococcus aureus V8 protease
    • Chobert, J.-M.; Sitohy, M. Z.; Whitaker, J. R. Solubility and emulsifying properties of caseins modified enzymatically by Staphylococcus aureus V8 protease. J. Agric. Food Chem. 1988, 36, 220-224.
    • (1988) J. Agric. Food Chem. , vol.36 , pp. 220-224
    • Chobert, J.-M.1    Sitohy, M.Z.2    Whitaker, J.R.3
  • 8
    • 0001467082 scopus 로고    scopus 로고
    • Study of putative glycosylation sites in bovine β-casein introduced by PCR-based site-directed mutagenesis
    • Choi, B. K.; Jiménez-Flores, R. Study of putative glycosylation sites in bovine β-casein introduced by PCR-based site-directed mutagenesis. J. Agric. Food Chem. 1996, 44, 358-364.
    • (1996) J. Agric. Food Chem. , vol.44 , pp. 358-364
    • Choi, B.K.1    Jiménez-Flores, R.2
  • 9
    • 0002330421 scopus 로고
    • Covalent binding of glycosyl residues to bovine casein: Effects on solubility and viscosity
    • Courthaudon, F. L.; Colas, B.; Lorient, D. Covalent binding of glycosyl residues to bovine casein: effects on solubility and viscosity. J. Agric. Food Chem. 1989, 37, 32-36.
    • (1989) J. Agric. Food Chem. , vol.37 , pp. 32-36
    • Courthaudon, F.L.1    Colas, B.2    Lorient, D.3
  • 11
    • 0040953119 scopus 로고
    • Modification of proteins
    • Advances in Chemistry Series 198; American Chemical Society: Washington, DC
    • Feeney, R. E.; Whitaker, J. R. Modification of proteins. In Food, Nutritional, and Pharmacological Aspects; Advances in Chemistry Series 198; American Chemical Society: Washington, DC, 1982.
    • (1982) Food, Nutritional, and Pharmacological Aspects
    • Feeney, R.E.1    Whitaker, J.R.2
  • 12
    • 0025367812 scopus 로고
    • Sequence differences between glycosylated and non-glycosylated Asn-X-Thr/Ser acceptor sites: Implication for protein engineering
    • Gavel, Y.; von Heijin, G. Sequence differences between glycosylated and non-glycosylated Asn-X-Thr/Ser acceptor sites: implication for protein engineering. Protein Eng. 1990, 3, 433-442.
    • (1990) Protein Eng. , vol.3 , pp. 433-442
    • Gavel, Y.1    Von Heijin, G.2
  • 15
    • 0001615952 scopus 로고
    • Expression of bovine β-casein in Saccharomyces cerevisiae and characterization of the protein in vivo
    • Jiménez-Flores, R.; Richardson T.; Bisson, L. Expression of bovine β-casein in Saccharomyces cerevisiae and characterization of the protein in vivo. J. Agric. Food Chem. 1990, 38, 1134-1141.
    • (1990) J. Agric. Food Chem. , vol.38 , pp. 1134-1141
    • Jiménez-Flores, R.1    Richardson, T.2    Bisson, L.3
  • 16
    • 0000310789 scopus 로고
    • Functional casein-polysaccharide conjugates prepared by controlled dry heating
    • Kato, A.; Mifuru, R.; Matsudomi, N.; Kobayashi, K. Functional casein-polysaccharide conjugates prepared by controlled dry heating. Biosci., Biotechnol., Biochem. 1992, 56, 567-571.
    • (1992) Biosci., Biotechnol., Biochem. , vol.56 , pp. 567-571
    • Kato, A.1    Mifuru, R.2    Matsudomi, N.3    Kobayashi, K.4
  • 17
    • 0018319580 scopus 로고
    • Chemical modification for improving functional properties of plant and yeast proteins
    • ACS Symposium Series 92; Pour-El, A., Ed.; American Chemical Society: Washington, DC
    • Kinsella, J. E.; Shetty, J. K. Chemical modification for improving functional properties of plant and yeast proteins. In Functionality and Protein Structure; ACS Symposium Series 92; Pour-El, A., Ed.; American Chemical Society: Washington, DC, 1979; pp 37-64.
    • (1979) Functionality and Protein Structure , pp. 37-64
    • Kinsella, J.E.1    Shetty, J.K.2
  • 18
    • 0014949207 scopus 로고
    • Change of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. Change of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970, 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 19
    • 0001227441 scopus 로고
    • Enhancing the gelation of β-lactoglobulin
    • Lee, S.-P.; Cho, S.; Batt, C. A. Enhancing the gelation of β-lactoglobulin. J. Agric. Food Chem. 1993, 41, 1343-1348.
    • (1993) J. Agric. Food Chem. , vol.41 , pp. 1343-1348
    • Lee, S.-P.1    Cho, S.2    Batt, C.A.3
  • 20
    • 0024780463 scopus 로고
    • Milk protein typing of bovine mammary gland tissue used to generate a complementary deoxyribonucleic acid library
    • Medrano, J. F.; Sharrow, L. Milk protein typing of bovine mammary gland tissue used to generate a complementary deoxyribonucleic acid library. J. Dairy Sci. 1989, 72, 3190-3196.
    • (1989) J. Dairy Sci. , vol.72 , pp. 3190-3196
    • Medrano, J.F.1    Sharrow, L.2
  • 21
    • 0001952063 scopus 로고
    • Production and use of milk proteins in food
    • Morr, C. V. Production and use of milk proteins in food. Food Technol. 1984, 38, 39-48.
    • (1984) Food Technol. , vol.38 , pp. 39-48
    • Morr, C.V.1
  • 22
    • 0001526017 scopus 로고
    • Genetic engineering of bovine κ-casein to improve its nutritional quality
    • Oh, S.; Richardson, T. Genetic engineering of bovine κ-casein to improve its nutritional quality. J. Agric. Food Chem. 1991, 39, 422-427.
    • (1991) J. Agric. Food Chem. , vol.39 , pp. 422-427
    • Oh, S.1    Richardson, T.2
  • 23
    • 2842610321 scopus 로고
    • Expression of biomedical proteins in milk of transgenic animals
    • Plantenburg, G. J.; Kirmpenfort, P.; Kooiman, P.; Kootwijk, H. Expression of biomedical proteins in milk of transgenic animals. J. Cell. Biochem. 1991, Suppl. 15A, 210-210.
    • (1991) J. Cell. Biochem. , Issue.SUPPL. 15A , pp. 210-210
    • Plantenburg, G.J.1    Kirmpenfort, P.2    Kooiman, P.3    Kootwijk, H.4
  • 24
    • 0024672126 scopus 로고
    • Structural requirements for protein N-glycosylation
    • Roitsch, T.; Lehle, L. Structural requirements for protein N-glycosylation. Eur. J. Biochem. 1989, 181, 525-529.
    • (1989) Eur. J. Biochem. , vol.181 , pp. 525-529
    • Roitsch, T.1    Lehle, L.2
  • 25
    • 0019154834 scopus 로고
    • Differences in glycosylation patterns of closely related murin e leukemia viruses
    • Rosner, M. R.; Grinna, L. S.; Robbins, P. W. Differences in glycosylation patterns of closely related murin e leukemia viruses. Proc. Natl. Acad. Sci. U.S.A. 1980, 77, 67-71.
    • (1980) Proc. Natl. Acad. Sci. U.S.A. , vol.77 , pp. 67-71
    • Rosner, M.R.1    Grinna, L.S.2    Robbins, P.W.3
  • 28
    • 0023646640 scopus 로고
    • Alteration of the quality of milk by expression of sheep β-lactoglobulin in transgenic mice
    • Simons, J. P.; McClenaghan, M.; Clark, A. J. Alteration of the quality of milk by expression of sheep β-lactoglobulin in transgenic mice. Nature 1987, 328, 530-532.
    • (1987) Nature , vol.328 , pp. 530-532
    • Simons, J.P.1    McClenaghan, M.2    Clark, A.J.3
  • 29
    • 0026537624 scopus 로고
    • Expression analysis of ruminant α-lactalbumin in transgenic mice: Developmental regulation and general location of important cis-regulatory elements
    • Soulier, S.; Vilotte, J. L.; Stinnakre, M. G.; Mercier, J.-C. Expression analysis of ruminant α-lactalbumin in transgenic mice: developmental regulation and general location of important cis-regulatory elements. FEBS Lett. 1992, 297, 13-17.
    • (1992) FEBS Lett. , vol.297 , pp. 13-17
    • Soulier, S.1    Vilotte, J.L.2    Stinnakre, M.G.3    Mercier, J.-C.4
  • 30
    • 0026458351 scopus 로고
    • Assaying glycoprotein hormones: The influence of glycosylation on immunoreactivity
    • Stoning, P. L. Assaying glycoprotein hormones: the influence of glycosylation on immunoreactivity. Trends Biotechnol. 1992, 10, 427-432.
    • (1992) Trends Biotechnol. , vol.10 , pp. 427-432
    • Stoning, P.L.1
  • 31
    • 0002772383 scopus 로고
    • Chemistry of the caseins
    • Fox, P. F., Ed.; Elsevier Applied Science: New York
    • Swaisgood, H. E. Chemistry of the caseins. In Advanced Dairy Chemistry-1: Protein; Fox, P. F., Ed.; Elsevier Applied Science: New York, 1992; pp 63-110.
    • (1992) Advanced Dairy Chemistry-1: Protein , pp. 63-110
    • Swaisgood, H.E.1
  • 32
    • 0024790207 scopus 로고
    • Efficient tissue-specific expression of bovine α-lactalbumin in transgenic mice
    • Vilotte, J. L.; Soulier, S.; Stinnakre, M.-G.; Massoud, M. Efficient tissue-specific expression of bovine α-lactalbumin in transgenic mice. Eur. J. Biochem. 1989, 186, 43-48.
    • (1989) Eur. J. Biochem. , vol.186 , pp. 43-48
    • Vilotte, J.L.1    Soulier, S.2    Stinnakre, M.-G.3    Massoud, M.4
  • 33
    • 0019065845 scopus 로고
    • Carbohydrate composition of the oligosaccharide units of the haemagglutinin from the Hong Kong influenza virus A/Memphis/102/ 72
    • Ward, C. W.; Gleeson, P. A.; Dopheide, T. A. Carbohydrate composition of the oligosaccharide units of the haemagglutinin from the Hong Kong influenza virus A/Memphis/102/ 72. Biochem. J. 1980, 189, 649-652.
    • (1980) Biochem. J. , vol.189 , pp. 649-652
    • Ward, C.W.1    Gleeson, P.A.2    Dopheide, T.A.3
  • 34
    • 0039893454 scopus 로고
    • 1-casein cDNA under the control of MMTV promoter/enhancer in the milk of transgenic mice
    • 1-casein cDNA under the control of MMTV promoter/enhancer in the milk of transgenic mice. J. Cell. Biochem. 1991, Suppl. 15A, 213-213.
    • (1991) J. Cell. Biochem. , Issue.SUPPL. 15A , pp. 213-213
    • Yom, H.-C.1    Bremel, R.D.2    First, N.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.