Abstract
Transgenic animals are a useful in vivo experimental model for assessing the ability and impact of foreign gene expression in a biological system. Transgenic mice are most commonly used, while transgenic steep, goats, pigs and cows have also been developed for specific, “applied” purposes. Most of the work directed at targeting expression of transgenes to the mammary gland of an animal, by using a milk gene promoter, has been with the intent of either studying promoter function or recovering the desired protein from the milk. Transgenic technology can also be used to alter the functional and physical properties of milk resulting in novel manufacturing properties. The properties of milk have been altered by adding a new protein with the aim of improving the milk, not of recovering the protein for other uses.
This is a preview of subscription content, access via your institution
Access options
Subscribe to this journal
Receive 12 print issues and online access
$209.00 per year
only $17.42 per issue
Buy this article
- Purchase on Springer Link
- Instant access to full article PDF
Prices may be subject to local taxes which are calculated during checkout
Similar content being viewed by others
References
Mercier, J.C. and Vilotte, J.L. 1993. Structure and function of milk protein genes. J. Dairy Sci. 76: 3079–3098.
Bawden, W.S., Passey, R.J. and Mackinlay, A.G. 1994. The genes encoding the major milk specific proteins and their use in transgenic studies and protein engineering. Biotech. Gen. Eng. Rev. 12: 89–137.
Wilmut, I., Archibald, A.L., McClenaghan, M., Simons, J.P., Whitelaw, C.B.A. and Clark, A.J. 1991. Production of pharmaceutical proteins in milk. Experientia 47: 905–912.
Fennema, O.R. 1985. In: Food Chemistry, 2nd Edition, Fennema, O. R. (Ed.). M. Dekker, New York.
Threadgill, D.W. and Womack, J.E. 1990. Genomic analysis of the major bovine milk protein genes. Nucleic Acids Res. 23: 6935–6942.
Lee, L.-Y. and Rosen, J.M. 1988. A transfected α-casein minigene bypasses post-transcriptional control by hormones, but retains cell-substratum regulation in mammary epithelial cells. Mol. Endocrinol. 2: 431–443.
Koczan, D., Hobom, G. and Seyfert, H.-M. 1991. Genomic organization of the bovine αs1-casein gene. Nucleic Acids Res. 19: 5591–5596.
Jolivet, G., Devinoy, E., Fontaine, M.L. and Houdebine, L.M. 1992. Structure of the gene encoding rabbit αs1-casein. Gene 113: 257–262.
Groenen, M.A.M., Dijkhof, R.J.M., Verstege, A.J.M. and van der Poel, J.J. 1993. The complete sequence of the gene encoding bovine αs2-casein. Gene 123: 187–193.
Bonsing, J., Ring, J.M., Stewart, A.F. and Mackinlay, A.G. 1988. Complete nucleotide sequence of the bovine β-casein gene. Aust. J. Biol. Sci. 41: 527–537.
Gorodetsky, S.I., Tkach, T.M. and Kapelinskaya, T.V. 1988. Isolation and characterization of the Bos taunts β-casein gene. Gene 66: 87–96.
Roberts, B., DiTullio, P., Vitale, J., Hehir, K. and Gordon, K. 1992. Cloning of the goat β-casein encoding gene and expression in transgenic mice. Gene 121: 255–262.
Jones, W.K., Yu-Lee, L.-Y., Clift, S.M., Brown, T.L. and Rosen, J.M. 1985. The rat casein multigene family. Fine structure and evolution of the β-casein gene. J. Biol. Chem. 260: 7042–7050.
Yoshimura, M. and Oka, T. 1989. Isolation and structural analysis of the mouse β-casein gene. Gene 78: 267–275.
Thepot, D., Devinoy, E., Fontaine, M.L. and Houdebine, L.M. 1991. Structure of the gene encoding rabbit β-casein. Gene 97: 301–306.
Hansson, L., Edlund, A., Johansson, T., Hernell, O., Stromquist, M., Lindquist, S., Lonnerdal, B. and Bergstrom, S. 1994. Structure of the human β-casein encoding gene. Gene 13: 193–199.
Alexander, J., Stewart, A.F., Mackinlay, A.G., Kapelinskaya, T.V., Tkach, M. and Gorodetsky, S.I. 1988. Isolation and characterization of the bovine κ-casein gene. Biochem. J. 178: 395–401.
Thompson, M.D., Dave, J.R. and Nakhasi, H.L. 1985. Molecular cloning of mouse mammary gland κ-casein: comparison with rat κ-casein and rat and human γ-fibrinogen. DNA 4: 263–271.
Hall, L., Emery, D.C., Davies, M.S., Parker, D. and Craig, R.K. 1987. Organization and sequence of the human α-lactalbumin gene. Biochem. J. 242: 735–742.
Quasba, P.K. and Safaya, S.K. 1984. Similarity of the nucleotide sequences of the rat α-lactalbumin and chicken lysozyme genes. Nature 308: 377–380.
Vilotte, J.L. and Soulier, S. 1992. Isolation and characterization of the mouse α-lactalbumin-encoding gene: interspecies comparison, tissue- and stage-specific expression. Gene 119: 287–292.
Vilotte, J.L., Soulier, S., Merrier, J.C., Gaye, P., Hue-Delahaie, D. and Furet, J.P. 1987. Complete nucleotide sequence of bovine α-lactalbumin gene. Comparison with its rat counterpart. Biochimie 69: 609–620.
Vilotte, J.L., Soulier, S., Printz, C. and Mercier, J.C. 1991. Sequence of the goat α-lactalbumin-encoding gene: comparison with the bovine gene and evidence of related sequences in the goat genome. Gene 98: 271–276.
Laird, J.E., Lack, L., Hall, L., Boulton, A., Parker, D. and Craig, R.K. 1988. Structure and expression of the guinea pig α-lactalbumin gene. Biochem. J. 254: 85–94.
Harris, S., Ali, S., Anderson, S., Archibald, A.L. and Clark, A.J. 1988. Complete nucleotide sequence of the ovine β-lactoglobulin gene. Nucleic Acids Res. 16: 10379–10380.
Watson, C.J., Gordon, K.E., Robertson, M. and Clark, A.J. 1991. Interaction of DNA binding proteins with a milk protein gene promoter in vitro: identification of a mammary gland-specific factor. Nucleic Acids Res. 19: 6603–6610.
Alexander, L.J., Hayes, G., Bawden, W., Stewart, A.F. and Mackinlay, A.G. 1993. Complete nucleotide sequence of the bovine β-lactoglobulin gene. Animal Biotech. 4: 110.
Hennighausen, L.G. and Sippel, A.E. 1982. Characterization and cloning of the mRNAs specific for the lactating mouse mammary gland. Eur. J. Biochem. 125: 131–141.
Campbell, S.M. and Rosen, J.M. 1984. Comparison of the whey acidic protein genes of the rat and mouse. Nucleic Acids Res. 12: 8685–8696.
Thepot, D., Devinoy, E., Fontaine, M.L. and Houdebine, L.M. 1991. Complete sequence of the rabbit whey acidic protein gene. Nucleic Acids Res. 18: 3641.
Bayna, E.M. and Rosen, J.M. 1990. Tissue specific expression of the rat whey acidic protein gene in transgenic mice. Nucleic Acids Res. 18: 2977–2985.
Andres, A.-C., Schonenberger, C.-A., Groner, B., Hennighausen, L., LeMeur, M. and Gerlinger, P. 1987. Ha-ras oncogene expression directed by a milk protein gene promoter: Tissue specificity, hormonal regulation, and tumor induction in transgenic mice. Proc. Natl. Acad. Sci. USA 84: 1299–1303.
Gorden, K., Lee, E., Vitale, J.A., Smith, A.E., Westphal, H. and Hennighausen, L. 1987. Production of human tissue plasminogen activator in transgenic mouse milk. Bio/Technology 5: 1183–1187.
Ebert, K.M., Selgrath, J.P., DiTullio, P., Denman, J., Smith, T.E., Memon, M.A., Schindler, J.E., Monastersky, G.M., Vitale, J.A. and Gorden, K. 1991. Transgenic production of a variant of human tissue type plasminogen activator in goat milk: Generation of transgenic goats and analysis of expression. Bio/Technology 9: 835–838.
Wall, R.J., Pursel, V.G., Shamay, A., McKnight, R.A., Pittius, C.W. and Hennighausen, L. 1991. High level synthesis of a heterologous milk protein in the mammary glands of transgenic swine. Proc. Natl. Acad. Sci. USA 88: 1696–1700.
Hansson, L., Edlund, M., Edlund, A., Johansson, T., Marklund, S.L., Fromm, S., Stromqvist, M. and Tornell, J. 1994. Expression and characterization of biologically active human extracellular superoxide dismutase in milk of transgenic mice. J. Biol. Chem. 69: 5358–5363.
Velander, W.H., Page, R.L., Morcol, T., Russell, C.G., Canseco, R., Young, J.M., Drohan, W.N., Gwazdauskas, F.C., Wilkins, T.D. and Johnson, J.L. 1992. Production of biologically active protein C in the milk of transgenic mice. Ann. N. Y. Acad. Sci. 665: 391–403.
Velander, W.H., Johnson, J.L., Page, R.L., Russell, C.G., Subramanian, A., Wilkins, T.D., Gwazdauskas, F.C., Pittius, C. and Drohan, W.N. 1992. High-level expression of a heterologous protein in the milk of transgenic swine using the cDNA encoding human protein C. Proc. Natl. Acad. Sci. USA 89: 12003–12007.
Drohan, W.N., Zhang, D., Paleyanda, R.K., Chang, R., Wroble, M., Velander, W. and Lubon, H. 1994. Inefficient processing of human protein C in the mouse mammary gland. Transgenic Res. 3: 355–364.
Bischoff, R., Degryse, E., Perraud, E., Dalemans, W., Ali-Hadji, D., Thepot, D., Devinoy, E., Houdebine, L.M. and Pavirani, A. 1992. A 17.6 kbp region located upstream of the rabbit WAP gene directs high level expression of a functional human protein variant in transgenic mouse milk. FEBS 305: 265–268.
Devinoy, E., Thepot, D., Stinnakre, M.-G., Fontaine, M.-L., Grabowski, H., Puissant, C., Pavirani, A. and Houdebine, L.-M. 1994. High level production of human growth hormone in the milk of transgenic mice: the upstream region of the rabbit whey acidic protein (WAP) gene targets transgene expression to the mammary gland. Transgenic Res. 3: 79–89.
Maschio, A., Brickell, P.M., Kioussis, D., Mellor, A.L., Katz, D. and Graig, R.K. 1991. Transgenic mice carrying the guinea-pig α-lactalbumin gene transcribe milk protein genes in their sebaceous glands during lactation. Biochem. J. 275: 459–467.
Bleck, G.T. and Bremel, R.D. 1993. Variation in expression of a bovine α-lactalbumin transgene in milk of transgenic mice. J. Dairy Sci. 77: 1897–1904.
Vilotte, J.L., Soulier, S., Stinnakre, M.G., Massoud, M. and Mercier, J.C. 1989. Efficient tissue-specific expression of bovine α-actalbumin in transgenic mice. Eur. J. Biochem. 186: 43–48.
Soulier, S., Vilotte, J.L., Stinnakre, M.G. and Mercier, J.C. 1992. Expression analysis ruminant α-lactalbumin in transgenic mice: developmental regulation and general location of important cis-egulatory elements. FEBS 297: 13–18.
Simons, J.P., McClenaghan, M. and Clark, A.J. 1987. Alteration of the quality of milk by expression of sheep β-lactoglobulin in transgenic mice. Nature 328: 530–532.
Archibald, A.L., McClenaghan, M., Hornsey, V., Simons, J.P. and Clark, A.J. 1990. High level expression of biologically active human α1-antitrypsin in the milk of transgenic mice. Proc. Natl. Acad. Sci. USA 87: 5178–5182.
Wright, G., Carver, A., Cottom, D., Reeves, D., Scott, A., Simons, P., Wilmut, I., Garner, I. and Colman, A. 1991. High level expression of active human α1-antitrypsin in the milk of transgenic sheep. Bio/Technology 9: 830–834.
Shani, M., Barash, I., Nathan, M., Ricca, G., Searfoss, G.H., Dekel, I., Faerman, A., Givol, D. and Hurwitz, D.R. 1992. Expression of human serum albumin in the milk of transgenic mice. Transgenic Res. 1: 195–208.
Lee, K.-F., DeMayo, F.J., Atiee, S.H. and Rosen, J.M. 1988. Tissue specific expression of the rat β-casein gene in transgenic mice. Nucleic Acids Res. 16: 1027–1041.
Lee, K.-F., Atiee, S.H. and Rosen, J.M. 1989. Differential regulation of rat β-casein-chloramphenicol acetyltransferase fusion gene expression in transgenic mice. Mol. Cell Biol. 9: 560–565.
Buhler, T.A., Bruyere, T., Went, D.E., Stranzinger, G. and Burki, K. 1990. Rabbit β-casein promoter directs secretion of human interleukin-2 into the milk of transgenic rabbits. Bio/Technology 8: 140–143.
Persuy, M.-A., Stinnakre, M.-G., Printz, C., Mahe, M.-F. and Mercier, J.C. 1992. High expression of the caprine β-casein gene in transgenic mice. Eur. J. Biochem. 205: 887–893.
DiTullio, P., Cheng, S.H., Marshall, J., Gregory, R.J., Ebert, K.M., Meade, H.M. and Smith, A.E. 1992. Production of cystic fibrosis transmembrane conductance regulator in the milk of transgenic mice. Bio/Technology 10: 74–77.
Gutierrez, A., Meade, H.M., Jimenez-Flores, R., Anderson, G.B., Murray, J.D. and Medrano, J.F. 1995. Expression analysis of bovine κ-casein in the mammary gland of transgenic mice. Transgenic Res. In press.
Clarke, R.A., Sokol, D., Rigby, N., Ward, K., Murray, J.D. and Mackinlay, A.G. 1994. Mammary gland specific expression of bovine αs1-casein derived transgenes in mice. Transgenics 1: 313–319.
Brem, G., Haiti, P., Besenfelder, U., Wolf, E., Zinovieva, N. and Pfaller, R. 1994. Expression of synthetic cDNA sequences encoding human insulin-like growth factor-1 (IGF-1) in the mammary gland of transgenic rabbits. Gene 149: 351–355.
Meade, H., Gates, L., Lacy, E. and Lonberg, N. 1990. Bovine αs1-casein gene sequences direct high level expression of active human urokinase in mouse milk. Bio/Technology 8: 443–446.
Maga, E.A., Anderson, G.B., Huang, M.C. and Murray, J.D. 1994. Expression of human lysozyme mRNA in the mammary gland of transgenic mice. Transgenic Res. 3: 36–42.
Platenburg, G.J., Kootwijk, E.P.A., Kooiman, P.M., Woloshuk, S.L., Nuijens, J.H., Krimpenfort, P.J.A., Pieper, F.R., de Boer, H.A. and Strijker, R. 1994. Expression of human lactoferrin in milk of transgenic mice. Transgenic Res. 3: 99–108.
Krimpenfort, P., Rademakers, A., Eyestone, W., van der Schans, A., van den Broek, S., Kooiman, P., Kootwijk, E., Platenburg, G., Pieper, F., Strijker, R. and de Boer, H. 1991. Generation of transgenic dairy cattle using in vitro embryo production. Bio/Technology 9: 844–847.
Whitelaw, C.B.A., Archibald, A.L., Harris, S., McClenaghan, M., Simons, J.P. and Clark, A.J. 1991. Targeting expression to the mammary gland: intronic sequences can enhance the efficiency of gene expression in transgenic mice. Transgenic Res. 1: 3–13.
Hurwitz, D.R., Nathan, M., Barash, I., Ilan, N. and Shani, M. 1994. Specific combinations of human serum albumin introns direct high level expression of albumin in transfected COS cells and in the milk of transgenic mice. Transgenic Res. 3: 365–375.
Webb, B.H., Johnson, A.H. and Alford, J.A. 1974. In: Fundamentals in Dairy Chemistry, 2nd Edition, Webb, B. H., Johnson, A. H. and Alford, J. A. (Eds.). AVI Publishing Co. Inc., Westport, Connecticut.
Fox, P.F. 1982. Chemistry of milk protein. Vols. 1 and 2 In: Developments in Dairy Chemistry, Fox, P. F. (Ed.). Applied Sci. Pub., New York.
Mercier, J.C. 1981. Phosphorylation of caseins: evidence for an amino acid triplet code posttranslationally recognized by specific kinases. Biochimie 63: 1–17.
Holt, C. 1992. Structure and stability of bovine casein micelles. Adv. in Prot. Chem. 43: 63–157.
Phillips, D.C. 1966. The 3-dimensional structure of an enzyme molecule. Sci. Am. 215: 78–90.
Jolles, P. and Jolles, J. 1984. What's new in lysozyme research. Mol. and Cell. Biochem. 63: 165–189.
Fleming, A. 1922. On a remarkable bacteriolytic element found in tissues and secretions. Proc. Roy. Soc. London Ser. B 93: 306–317.
Dobson, D.E., Prager, E.M. and Wilson, A.C. 1984. Stomach lysozyme of ruminants, I. Distribution and catalytic properties. J. Biol. Chem. 259: 11607–11616.
Costerton, J.W., Ingram, J.M. and Chang, K.J. 1974. Structure and function of the cell envelope of bacteria. Bacteriol. Rev. 38: 87–110.
Smith, G.N. and Stoker, C. 1949. Inhibition of crystalline lysozyme. Arch. Biochem. 21: 383.
Chandan, R.C., Parry, R.M. and Shahani, K.M. 1968. Lysozyme, lipase, and ribonuclease in milk of various species. J. Dairy Sci. 51: 606–607.
Vakil, J.R., Chandan, R.C., Parry, R.M. and Shahani, K.M. 1970. Susceptibility of several microorganisms to milk lysozymes. J. Dairy Sci. 52: 1192–1197.
Chang, S.S. 1990. Antimicrobial proteins of maternal and cord sera and human milk in relation to maternal nutritional studies. Am. J. Clin. Nutr. 51: 183–187.
Hughey, V.L., Wilger, P.A. and Johnson, E.A. 1989. Antibacterial activity of hen egg white lysozyme against Listeria monocytogenes ScottA in foods. Appl. Environ. Microbiol. 55: 631–638.
Hughey, V.L. and Johnson, E.A. 1987. Antimicrobial activity of lysozyme against bacteria involved in food spoilage and food borne disease. Appl. Environ. Microbiol. 53: 2165–2170.
Panfil-Kuncewicz, H. and Kisza, J. 1976. Studies on the lysozyme content of human and cow milk. Zesz. Nauk. Akad. Roln.-Tech. Olsztynie, Technol. Zywn. 8: 105–112.
Grinde, B. 1989. A lysozyme isolated from rainbow trout acts on mastitis pathogens. FEMS Micro. Letters 60: 179–182.
Redhead, K., Hill, T. and Mulloy, B. 1990. Antimicrobial effect of human milk on Bordetella pertussis . FEMS Micro. Letters 70: 179–182.
Carlsson, A., Bjorck, L. and Persson, K. 1989. Lactoferrin and lysozyme in milk during acute mastitis and their inhibitory effect in Delvotest P. J. Dairy Sci. 72: 3166–3175.
Hennart, P.F., Brasseur, D.J., Delogne-Desnoeck, J.B., Dramaix, M.M. and Robyn, C.E. 1991. Lysozyme, lactoferrin, and secretory immunoglobulin A content in breast milk: Influence of duration of lactation, nutritional status, prolactin status, and parity of mother. Am. J. Clin. Nutr. 53: 32–39.
Shahani, K.M., Chandan, R.C., Kelly, P.L. and MacQuiddy, E.L. 1962. Determination of lysozyme in milk and factors affecting its concentration and properties. Proc. 16th Intern. Dairy Congr. 8: 285–293.
Yoshida, A., Takagaki, Y. and Nishimune, T. 1991. Enzyme immunoassay for hen egg white lysozyme used as a food additive. J. Assoc. Off. Anal. Chem. 74: 502–505.
Osserman, E.F., Klockars, M., Halper, J. and Fischel, R.E. 1973. Effects of lysozyme on normal and transformed cells. Nature 243: 331.
Green, M.L. and Marshall, R.J. 1977. The acceleration by cationic materials of the coagulation of casein micelles by rennet. J. Dairy Res. 44: 521–531.
Pearce, K.N. 1976. Moving boundary electrophoresis of native and rennet-treated casein micelles. J. Dairy Res. 43: 27–36.
Marshall, R.J. and Green, M.L. 1980. The effect of the chemical structure of additives on the coagulation of casein micelle suspensions by rennet. J. Dairy Res. 47: 359–369.
DiGregorio, F. and Sisto, R. 1981. Milk coagulation by cationic polypeptides. J. Dairy Res. 48: 267–271.
Giangiacomo, R., Nigro, F., Messina, G. and Cattaneo, T.M.P. 1992. Lysozyme: just an additive or a technological aid as well? Food Additives and Contaminants 9: 427–433.
Waugh, D.F. 1971. Formation and structure of casein micelles, p. 3–85. In: Milk Proteins Chemistry and Molecular Biology, McKenzie, H. A. (Ed.). Academic Press, New York.
Schmidt, D.G. 1982. Association of caseins and casein micelle structure, p. 61–82, Vol. 1. In: Developments in Dairy Chemistry, Fox, P. F. (Ed.). Applied Sci Pub., New York.
Fox, P.F. 1982. Heat-induced coagulation of milk, p. 189–223, Vol. 1. In: Developments in Dairy Chemistry, Fox, P. F. (Ed.) Applied Sci. Pub., New York.
Jimenez-Flores, R. and Richardson, T. 1985. Genetic engineering of the caseins to modify the behavior of milk during processing: a review. J. Dairy Sci. 71: 2640–2654.
Clark, A.J. 1992. Prospects for the genetic engineering of milk. J. Cell Biochem. 49: 121–127.
Yom, H.G. and Bremel, R.D. 1993. Genetic engineering of milk composition: modification of milk components in lactating transgenic animals. Am. J. Clin. Nutr. Suppl. 8: 2995–3065.
Schaar, J. 1984. Effect of κ-casein genetic variants and lactation number on the renneting properties of individual milks. J. Dairy Res. 51: 97–406.
Marziali, A.S. and Ng-Kwan-Hang, K.F. 1986. Effect of milk composition and genetic polymorphism on coagulating properties of milk. J. Dairy Sci. 69: 1793–1798.
Conneely, O.M. and Headon, D.R. 1993. Lactoferrin, lactoperoxidase and lysozyme: nature's protective proteins, p. 123–131. In: Biotechnology in the Feed Industry, Proceedings of Alltech's Ninth Annual Symposium, Lyons, T. P. (Ed.). Alltech Tech. Pub., Nicholasville, KY.
Arnold, R.R., Cole, M.F. and McGhee, J.R. 1977. A bacteriocidal effect for human lactoferrin. Science 197: 263–265.
Kuizinga, A., vanHaeringen, N.J. and Kijlstra, A. 1987. Inhibition of hydroxyl radical formation by human tears. Invest. Ophthalmol. Vis. Sci. 28: 305–313.
Masson, P.L. and Heremans, J.F. 1971. Lactoferrin in milk from different species. Comp. Biochem. Physiol. 39B: 143–147.
Ellison, R.T. and Giehl, T.J. 1991. Killing gram-negative bacteria by lactoferrin and lysozyme. J. Clin. Invest. 88: 1080–1091.
Stuart, J., Norrell, S. and Harrington, J.P. 1984. Kinetic effect of human lactoferrin on the growth of Escherichia coli 0111. Int. J. Biochem. 16: 1043–1048.
Stephens, S., Dolby, J.M., Montreiul, J. and Spik, G. 1980. Differences in inhibition of the growth of commensal and enteropathogenic strains of Escherichia coli by lactoferrin and secretory immunoglobulinA isolated form human milk. Immunology. 41: 597–603.
Schulz-Lell, G., Dorner, K., Oldigs, H.-D., Sievers, E. and Scaule, E. 1991. Iron availability from an infant formula supplemented with bovine lactoferrin. Acta. Pediat. Scand. 80: 155–158.
Hekman, A.M. 1971. Association of lactoferrin with other proteins, as demonstrated by changes in electrophoretic mobility. Biochim. Biophys. Acta. 251: 380.
Maga, E.A., Anderson, G.B. and Murray, J.D. 1995. The effect of mammary gland expression of human lysozyme on the properties of milk in transgenic mice. J. Dairy Sci. In press.
Gutierrez, A., Maga, E.A., Meade, H.M., Shoemaker, C.F., Medrano, J.F., Anderson, G.B. and Murray, J.D. 1995. Alteration of physical characteristics of milk from bovine kappa-casein transgenic mice. J. Dairy Sci. Submitted.
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Maga, E., Murray, J. Mammary Gland Expression of Transgenes and the Potential for Altering the Properties of Milk. Nat Biotechnol 13, 1452–1457 (1995). https://doi.org/10.1038/nbt1295-1452
Issue Date:
DOI: https://doi.org/10.1038/nbt1295-1452
This article is cited by
-
Genetically engineered livestock for agriculture: a generation after the first transgenic animal research conference
Transgenic Research (2016)
-
Production of human lactoferrin and lysozyme in the milk of transgenic dairy animals: past, present, and future
Transgenic Research (2015)
-
Production of transgenic goats expressing human coagulation factor IX in the mammary glands after nuclear transfer using transfected fetal fibroblast cells
Transgenic Research (2013)
-
The extremely high level expression of human serum albumin in the milk of transgenic mice
Transgenic Research (2012)
-
High-level expression of bioactive recombinant human lysozyme in the milk of transgenic mice using a modified human lactoferrin BAC
Transgenic Research (2012)