Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
33
|
| pubmed:dateCreated |
1987-12-29
|
| pubmed:databankReference | |
| pubmed:abstractText |
Employing the rabbit liver progesterone-21-hydroxylase P-450 1 cDNA as a probe (Tukey, R.H., Okino, S., Barnes, H., Griffin, K.J., and Johnson, E.F. (1985) J. Biol. Chem. 260, 13347-13354), we have identified a highly homologous (81% within the coding region) human liver cDNA, termed Hp1-1, that encodes a 490-amino acid protein. Comparison of the predicted translation products between the human and rabbit homologues demonstrates that the two proteins are 73% homologous, while increasing to 82% similarity when allowing for conserved amino changes. The human P-450 1 is 82% homologous to the s-mephenytoin 4-hydroxylase (Umbenhauer, D. R., Martin, M. V., Lloyd, R. S., and Guengerich, F. P. (1987) Biochemistry 26, 1094-1099). Southern blot analysis using various portions of the human P-450 1 cDNA as probes indicates that the human P-450 1 gene is part of a larger gene family but can be selectively identified by using a 3'-noncoding portion of the cDNA. Identification of the gene from a panel of human-rodent somatic cell hybrids using the conserved 3' portion of the human P-450 1 cDNA as a probe places the location of the gene on human chromosome 10. Results are also presented which demonstrate that the human P-450 1 gene transcript is processed by an alternate RNA-splicing mechanism that generates two mRNA products, one which represents the functional transcript, and the other a form of mRNA that is not capable of encoding a functional P-450.
|
| pubmed:grant | |
| pubmed:commentsCorrections | |
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Cytochrome P-450 Enzyme System,
http://linkedlifedata.com/resource/pubmed/chemical/DNA,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/Steroid 21-Hydroxylase,
http://linkedlifedata.com/resource/pubmed/chemical/Steroid Hydroxylases
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Nov
|
| pubmed:issn |
0021-9258
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
25
|
| pubmed:volume |
262
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
16072-9
|
| pubmed:dateRevised |
2007-11-14
|
| pubmed:meshHeading |
pubmed-meshheading:3500169-Amino Acid Sequence,
pubmed-meshheading:3500169-Animals,
pubmed-meshheading:3500169-Base Sequence,
pubmed-meshheading:3500169-Chromosome Mapping,
pubmed-meshheading:3500169-Chromosomes, Human, Pair 10,
pubmed-meshheading:3500169-Cloning, Molecular,
pubmed-meshheading:3500169-Cytochrome P-450 Enzyme System,
pubmed-meshheading:3500169-DNA,
pubmed-meshheading:3500169-Genes,
pubmed-meshheading:3500169-Humans,
pubmed-meshheading:3500169-Liver,
pubmed-meshheading:3500169-Molecular Sequence Data,
pubmed-meshheading:3500169-Plasmids,
pubmed-meshheading:3500169-RNA, Messenger,
pubmed-meshheading:3500169-RNA Splicing,
pubmed-meshheading:3500169-Rabbits,
pubmed-meshheading:3500169-Steroid 21-Hydroxylase,
pubmed-meshheading:3500169-Steroid Hydroxylases,
pubmed-meshheading:3500169-Transcription, Genetic
|
| pubmed:year |
1987
|
| pubmed:articleTitle |
Characterization of multiple human cytochrome P-450 1 cDNAs. The chromosomal localization of the gene and evidence for alternate RNA splicing.
|
| pubmed:affiliation |
University of California at San Diego Cancer Center, Department of Medicine, La Jolla, 92093.
|
| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
|