Human hypoxanthine-guanine phosphoribosyltransferase: a single nucleotide substitution in cDNA clones isolated from a patient with Lesch-Nyhan syndrome (HPRTMidland)
dc.contributor.author | Davidson, Beverly L. | en_US |
dc.contributor.author | Palella, Thomas D. | en_US |
dc.contributor.author | Kelley, William N. | en_US |
dc.date.accessioned | 2006-04-07T20:13:33Z | |
dc.date.available | 2006-04-07T20:13:33Z | |
dc.date.issued | 1988-08-15 | en_US |
dc.identifier.citation | Davidson, 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.uri | http://www.sciencedirect.com/science/article/B6T39-47PHBTN-2T1/2/9614bf6f8b34d2e3ca08a220b69426b8 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/27178 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=3265398&dopt=citation | en_US |
dc.description.abstract | We 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.extent | 985352 bytes | |
dc.format.extent | 3118 bytes | |
dc.format.mimetype | application/pdf | |
dc.format.mimetype | text/plain | |
dc.language.iso | en_US | |
dc.publisher | Elsevier | en_US |
dc.title | Human hypoxanthine-guanine phosphoribosyltransferase: a single nucleotide substitution in cDNA clones isolated from a patient with Lesch-Nyhan syndrome (HPRTMidland) | en_US |
dc.type | Article | en_US |
dc.rights.robots | IndexNoFollow | en_US |
dc.subject.hlbsecondlevel | Molecular, Cellular and Developmental Biology | en_US |
dc.subject.hlbsecondlevel | Genetics | en_US |
dc.subject.hlbsecondlevel | Biological Chemistry | en_US |
dc.subject.hlbtoplevel | Science | en_US |
dc.subject.hlbtoplevel | Health Sciences | en_US |
dc.description.peerreviewed | Peer Reviewed | en_US |
dc.contributor.affiliationum | Departments 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.affiliationum | Departments 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.affiliationum | Departments 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.pmid | 3265398 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/27178/1/0000176.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1016/0378-1119(88)90601-4 | en_US |
dc.identifier.source | Gene | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
Files in this item
Remediation of Harmful Language
The University of Michigan Library aims to describe library materials in a way that respects the people and communities who create, use, and are represented in our collections. Report harmful or offensive language in catalog records, finding aids, or elsewhere in our collections anonymously through our metadata feedback form. More information at Remediation of Harmful Language.
Accessibility
If you are unable to use this file in its current format, please select the Contact Us link and we can modify it to make it more accessible to you.