Isolation and Characterization of a Full-Length Expressible cDNA for Human Hypoxanthine Phosphoribosyltransferase

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 se...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 1983-01, Vol.80 (2), p.477-481
Main Authors: Jolly, D. J., Okayama, H., Berg, P., Esty, A. C., Filpula, D., Bohlen, P., Johnson, G. G., Shively, J. E., Hunkapillar, T., Friedmann, T.
Format: Article
Language:English
Subjects:
Amino acids
CDNA libraries
Cell lines
Complementary DNA
DNA
Enzymes
Gels
Hypoxia
Plasmids
Transfection
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Summary: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.
ISSN:0027-8424
DOI:10.1073/pnas.80.2.477