K
Katherine Gordon
Researcher at Genzyme
Publications - 9
Citations - 1347
Katherine Gordon is an academic researcher from Genzyme. The author has contributed to research in topics: Transgene & Gene. The author has an hindex of 7, co-authored 9 publications receiving 1333 citations.
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Transgenic animals secreting desired proteins into milk
TL;DR: In this paper, the authors describe a sequence containing a gene encoding a protein, the gene being under the transcriptional control in the DNA sequence of a mammalian milk protein promoter which does not naturally control the transcription of the gene, such DNA sequence including DNA enabling secretion of the protein.
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Transgenic production of a variant of human tissue-type plasminogen activator in goat milk: generation of transgenic goats and analysis of expression.
Karl M. Ebert,James P. Selgrath,Paul Ditullio,Julie S. Denman,Thomas E. Smith,Mushtaq A. Memon,Joanne E. Schindler,Glen M. Monastersky,James A. Vitale,Katherine Gordon +9 more
TL;DR: The first successful production of transgenic goats that express a heterologous protein in their milk was reported in this article, where the first animal, a female, was mated and allowed to carry the pregnancy to term.
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Production of Human Tissue Plasminogen Activator in Transgenic Mouse Milk
TL;DR: In this article, an exogenous gene was expressed in the mammary epithelium of transgenic mice in the hope that the encoded protein would be secreted into milk, and the protein was found to be biologically active.
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A milk protein gene promoter directs the expression of human tissue plasminogen activator cDNA to the mammary gland in transgenic mice
Christoph W. Pittius,Lothar Hennighausen,Eric Lee,Heiner Westphal,Edward Nicols,Jim Vitale,Katherine Gordon +6 more
TL;DR: It is demonstrated that the WAP gene promoter can target the expression of a transgene to the mammary gland and that this expression is inducible during lactation.
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Transgenic expression of a variant of human tissue-type plasminogen activator in goat milk: purification and characterization of the recombinant enzyme.
Julie S. Denman,Michael L. Hayes,Christine O'Day,Tim Edmunds,Catherine Bartlett,Shirish Hirani,Karl M. Ebert,Katherine Gordon,John M. McPherson +8 more
TL;DR: Analysis of the transgenic protein indicated that it had a significantly different carbohydrate composition from the recombinant enzyme produced in mouse C127 cells, and molecular size analysis of the oligosaccharides confirmed their differences and showed that the mouse cell-derived preparation contained larger, complex-type N-linked oligOSaccharide structures than the material produced in goat mammary tissue.