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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
1
|
| pubmed:dateCreated |
1995-2-2
|
| pubmed:abstractText |
Human erythrocytes contain a nicotinamide adenine dinucleotide phosphate (NADP[H])-binding protein, FX, whose levels are significantly increased in erythrocytes from glucose-6-phosphate dehydrogenase (G6PD)-deficient individuals bearing the mediterranean variant of G6PD. Elucidation of the still unknown biologic functions of FX was approached by means of amino acid sequencing of its 25 tryptic peptides. Searching in the EMBL data bank allowed identification of extensive homology between these tryptic peptides and all sequence-aligned regions encompassing the complete structure of a putative protein encoded by the P35B gene in the mouse. This gene, which differs from the normal allele by a point mutation, has been previously cloned from a tum- variant of the murine tumor cell line P815, so defined because it is associated with low tumorigenicity compared with the progenitor P815. The reported P35B cDNA contains an open reading frame (ORF) of 813 bp and encodes a putative protein of 271 amino acids (30 kD), whereas FX protein is 320 amino acids in length (35.81 kD, in good agreement with previous studies). However, a single base shift at position 4,752 of the P35B gene suppresses the stop codon after Phe 271 and allows continuation of the ORF for up to 320 amino acids to reach the same length as FX. The remarkably high extent (92%) of homology indicates that erythrocyte FX protein is the human homolog of the P35B gene product.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
AIM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Surface,
http://linkedlifedata.com/resource/pubmed/chemical/Carbohydrate Epimerases,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/Ketone Oxidoreductases,
http://linkedlifedata.com/resource/pubmed/chemical/Nerve Tissue Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Syntaxin 1,
http://linkedlifedata.com/resource/pubmed/chemical/TSTA3 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Trypsin
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Jan
|
| pubmed:issn |
0006-4971
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
1
|
| pubmed:volume |
85
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
264-7
|
| pubmed:dateRevised |
2006-11-15
|
| pubmed:meshHeading |
pubmed-meshheading:7803801-Amino Acid Sequence,
pubmed-meshheading:7803801-Animals,
pubmed-meshheading:7803801-Antigens, Surface,
pubmed-meshheading:7803801-Carbohydrate Epimerases,
pubmed-meshheading:7803801-Carrier Proteins,
pubmed-meshheading:7803801-DNA, Complementary,
pubmed-meshheading:7803801-Erythrocytes,
pubmed-meshheading:7803801-Glucosephosphate Dehydrogenase Deficiency,
pubmed-meshheading:7803801-Humans,
pubmed-meshheading:7803801-Ketone Oxidoreductases,
pubmed-meshheading:7803801-Mice,
pubmed-meshheading:7803801-Molecular Sequence Data,
pubmed-meshheading:7803801-Nerve Tissue Proteins,
pubmed-meshheading:7803801-Peptide Fragments,
pubmed-meshheading:7803801-Point Mutation,
pubmed-meshheading:7803801-Sequence Alignment,
pubmed-meshheading:7803801-Syntaxin 1,
pubmed-meshheading:7803801-Trypsin
|
| pubmed:year |
1995
|
| pubmed:articleTitle |
Primary structure of human erythrocyte nicotinamide adenine dinucleotide phosphate (NADP[H])-binding protein FX: identification with the mouse tum- transplantation antigen P35B.
|
| pubmed:affiliation |
Institute of Protein Biochemistry and Enzymology, National Research Council, Naples, Italy.
|
| pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
|