Published June 15, 1983
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Isolation and Characterization of a Full-Length Expressible cDNA for Human Hypoxanthine Phosphoribosyltransferase
Abstract
We have cloned a full-length 1.6-kilobase cDNA of a human mRNA coding for hypoxanthine phosphoribosyltransferase (HPRT; IMP:pyrophosphate phosphoribosyltransferase, EC 2.4.2.8) into a simian virus 40-based expression vector and have determined its full nucleotide sequence. The inferred amino acid sequence agrees with a partial amino acid sequence determined for authentic human HPRT protein. Transfection of HPRT-deficient mouse LA9 cells with the purified plasmid leads to the expression of human HPRT enzyme activity in cells stably transfected and selected for enzyme activity in hypoxanthine/aminopterin/thymidine medium.
Additional Information
Copyright © 1983 by the National Academy of Sciences Communicated by J. Edwin Seegmiller, October 7, 1982 T.F. thanks Dr. Wm. Nyhan for his interest and support. We thank Dorothy Miller for her administrative assistance during this work. This work was supported by grants from the Kroc Foundation, Santa Ynez; CA, and the Leon Gould Foundation, Tamarac, FL, and by National Institutes of Health Grants GM28223 and 1 RP1 CA31928-01. D.F. was supported by Public Health Service Fellowship Training Grant CA09290. The publication costs of this article were defrayed in part by page charge payment. This article must therefore be hereby marked "advertisement" in accordance with 18 U. S. C. §1734 solely to indicate this fact.Files
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