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Human hypoxanthine-guanine phosphoribosyltransferase: a single nucleotide substitution in cDNA clones isolated from a patient with Lesch-Nyhan syndrome (HPRTMidland)

dc.contributor.authorDavidson, Beverly L.en_US
dc.contributor.authorPalella, Thomas D.en_US
dc.contributor.authorKelley, William N.en_US
dc.date.accessioned2006-04-07T20:13:33Z
dc.date.available2006-04-07T20:13:33Z
dc.date.issued1988-08-15en_US
dc.identifier.citationDavidson, Beverly L., Palella, Thomas D., Kelley, William N. (1988/08/15)."Human hypoxanthine-guanine phosphoribosyltransferase: a single nucleotide substitution in cDNA clones isolated from a patient with Lesch-Nyhan syndrome (HPRTMidland)." Gene 68(1): 85-91. <http://hdl.handle.net/2027.42/27178>en_US
dc.identifier.urihttp://www.sciencedirect.com/science/article/B6T39-47PHBTN-2T1/2/9614bf6f8b34d2e3ca08a220b69426b8en_US
dc.identifier.urihttps://hdl.handle.net/2027.42/27178
dc.identifier.urihttp://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=3265398&dopt=citationen_US
dc.description.abstractWe have determined the molecular basis for hypoxanthine-guanine phosphoribosyltransferase (HPRT) deficiency in a patient J.H., with Lesch-Nyhan syndrome. Radioimmunoassay of lysates of erythrocytes or cultured B-lymphoblasts showed that this patient had no detectable HPRT enzyme activity or HPRT protein. HPRT-specific mRNA levels were normal by Northern analysis.We created a cDNA library from mRNA isolated from cultured lymphoblasts derived from this patient. Nucleotide sequencing of full-length HPRT cDNA clones revealed a single nucleotide (nt) substitution: a T-to-A transversion at nt 389. We have designated this variant HPRTMidland. The predicted amino acid (aa) substitution in HPRTMidland is a valine to aspartic acid at aa 130. This substitution is within 2 aa of the amino acid substitution in a previously defined HPRT variant, HPRTAnn Arbor. Both mutations are within a highly conserved sequence in the putative 5-phosphoribosyl-l-pyrophosphate-binding domain. The amino acid substitution in HPRTMidland causes a significant perturbation in the predicted secondary structure of this region. The HPRTMidland mutation affects a different domain of HPRT than the HPRTFlint mutation located at 167 nt away.en_US
dc.format.extent985352 bytes
dc.format.extent3118 bytes
dc.format.mimetypeapplication/pdf
dc.format.mimetypetext/plain
dc.language.isoen_US
dc.publisherElsevieren_US
dc.titleHuman hypoxanthine-guanine phosphoribosyltransferase: a single nucleotide substitution in cDNA clones isolated from a patient with Lesch-Nyhan syndrome (HPRTMidland)en_US
dc.typeArticleen_US
dc.rights.robotsIndexNoFollowen_US
dc.subject.hlbsecondlevelMolecular, Cellular and Developmental Biologyen_US
dc.subject.hlbsecondlevelGeneticsen_US
dc.subject.hlbsecondlevelBiological Chemistryen_US
dc.subject.hlbtoplevelScienceen_US
dc.subject.hlbtoplevelHealth Sciencesen_US
dc.description.peerreviewedPeer Revieweden_US
dc.contributor.affiliationumDepartments of Internal Medicine and Biological Chemistry and the Rackham Arthritis Research Unit, University of Michigan Medical School, Ann Arbor, MI 48109, U.S.A.en_US
dc.contributor.affiliationumDepartments of Internal Medicine and Biological Chemistry and the Rackham Arthritis Research Unit, University of Michigan Medical School, Ann Arbor, MI 48109, U.S.A.en_US
dc.contributor.affiliationumDepartments of Internal Medicine and Biological Chemistry and the Rackham Arthritis Research Unit, University of Michigan Medical School, Ann Arbor, MI 48109, U.S.A.en_US
dc.identifier.pmid3265398en_US
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/27178/1/0000176.pdfen_US
dc.identifier.doihttp://dx.doi.org/10.1016/0378-1119(88)90601-4en_US
dc.identifier.sourceGeneen_US
dc.owningcollnameInterdisciplinary and Peer-Reviewed


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