Production of Functional Human Hemoglobin in Transgenic Swine

• Published in: Bio/Technology 1992-05, Vol.10 (5), p.557-559
• Main Authors: Swanson, Mark E, Martin, Michael J, O'Donnell, J. Kevin, Hoover, Kathy, Lago, William, Huntress, Victoria, Parsons, Cynthia T, Pinkert, Carl A, Pilder, Stephen, Logan, John S
• Format: Article
• Language: English
• Subjects: Agriculture; Animals; Animals, Genetically Modified; Bioinformatics; Biological and medical sciences; Biomedical and Life Sciences; Biomedical Engineering/Biotechnology; Biomedicine; Biotechnology; Chromatography, DEAE-Cellulose; Chromosome Mapping; Fundamental and applied biological sciences. Psychology; Genetic engineering; Genetic technics; Globins - biosynthesis; Hemoglobins - biosynthesis; Hemoglobins - genetics; Hemoglobins - isolation & purification; Humans; Life Sciences; Methods. Procedures. Technologies; Microinjections; Oxygen - metabolism; research-paper; Swine; Transgenic animals; Transgenic animals and transgenic plants; Zygote - physiology
• ISSN: 0733-222X; 1087-0156; 2331-3684; 1546-1696
• DOI: 10.1038/nbt0592-557

A construct containing the locus control region (LCR) from the human β globin locus together with two copies of the human α 1 gene and a single copy of the human β A gene was used to obtain three transgenic pigs. The transgenic pigs are healthy, not anemic, and grow at a rate comparable to non–transgenic littermates. All animals expressed the human genes. However, α globin was consistently expressed at higher levels than β globin. Isolation of the human hemoglobin from both porcine hemoglobin and other non–hemoglobin proteins was accomplished by ion exchange chromatography. The purified porcine derived human hemoglobin exhibited an oxygen affinity similar to that of human derived human hemoglobin.