Synthesis of normal and variant human hypoxanthine-guanine phosphoribosyltransferase in Escherichia coli
dc.contributor.author | Davidson, Beverly L. | en_US |
dc.contributor.author | Brown, Jennifer E. | en_US |
dc.contributor.author | Weber, Christian H. | en_US |
dc.contributor.author | Palella, Thomas D. | en_US |
dc.contributor.author | Roessler, Blake J. | en_US |
dc.date.accessioned | 2006-04-10T15:54:48Z | |
dc.date.available | 2006-04-10T15:54:48Z | |
dc.date.issued | 1993-01-30 | en_US |
dc.identifier.citation | Davidson, Beverly L., Brown, Jennifer E., Weber, Christian H., Palella, Thomas D., Roessler, Blake J. (1993/01/30)."Synthesis of normal and variant human hypoxanthine-guanine phosphoribosyltransferase in Escherichia coli." Gene 123(2): 271-275. <http://hdl.handle.net/2027.42/31002> | en_US |
dc.identifier.uri | http://www.sciencedirect.com/science/article/B6T39-47PH7C3-1MP/2/5ad87b0d143f82b166270294865c00ab | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/31002 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=8428670&dopt=citation | en_US |
dc.description.abstract | Naturally occurring mutations in hypoxanthine-guanine phosphoribosyltransferase (HPRT) have been identified by amino acid sequencing, cDNA cloning, and direct nucleotide sequencing of PCR-amplified transcripts. To determine the effect these mutations have on the catalytic properties of the molecule, knowledge of the three-dimensional structure of HPRT is required. A prerequisite for this, however, is the availability of a large amount of purified product for crystallization and x-ray diffraction analysis. For these reasons we have developed an effective means of producing high levels of human HPRT in Escherichia coli using the expression cassette PCR. By taking advantage of a T7 polymerase/promoter system, we have expressed both normal and variant human hprt sequences in E. coli. The proteins synthesized from these sequences are immunologically and enzymatically active, and are physically indistinguishable from the HPRT in B-lymphoblasts derived from normal and three HPRT-deficient subjects. | en_US |
dc.format.extent | 830631 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 | Synthesis of normal and variant human hypoxanthine-guanine phosphoribosyltransferase in Escherichia coli | 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, University of Michigan Medical School, Ann Arbor, MI 48109, USA | en_US |
dc.contributor.affiliationum | Departments of Internal Medicine, University of Michigan Medical School, Ann Arbor, MI 48109, USA | en_US |
dc.contributor.affiliationum | Departments of Biological Chemistry, University of Michigan Medical School, Ann Arbor, MI 48109, USA | en_US |
dc.contributor.affiliationum | Departments of Internal Medicine, University of Michigan Medical School, Ann Arbor, MI 48109, USA | en_US |
dc.contributor.affiliationum | Departments of Internal Medicine, University of Michigan Medical School, Ann Arbor, MI 48109, USA | en_US |
dc.identifier.pmid | 8428670 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/31002/1/0000677.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1016/0378-1119(93)90137-R | en_US |
dc.identifier.source | Gene | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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