James, D C <br/><br/>
N-glycosylation of recombinant human interferon-gamma produced in different animal expression systems.  [electronic resource] 

 -  Bio/technology (Nature Publishing Company)  Jun 1995 
 - 592-6 p.  digital 
<br/><br/> Publication Type: Comparative Study; Journal Article; Research Support, Non-U.S. Gov't 
<br/><br/><label>ISSN: </label>0733-222X 
<br/><br/><label>Standard No.: </label>10.1038/nbt0695-592  doi 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Animals<br/>Baculoviridae<br/>CHO Cells<br/>Carbohydrate Conformation<br/>Cell Line<br/>Cricetinae<br/>Female<br/>Glycopeptides--analysis<br/>Glycosylation<br/>Humans<br/>Insecta--cytology<br/>Interferon-gamma--metabolism<br/>Mammary Glands, Animal--metabolism<br/>Mice<br/>Mice, Transgenic<br/>Oligosaccharides--analysis<br/>Recombinant Proteins<br/>Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization