rdf:type |
|
lifeskim:mentions |
umls-concept:C0003250,
umls-concept:C0031298,
umls-concept:C0032098,
umls-concept:C0038636,
umls-concept:C0204514,
umls-concept:C0205148,
umls-concept:C0560175,
umls-concept:C0870432,
umls-concept:C1555465,
umls-concept:C1705417,
umls-concept:C1706209
|
pubmed:issue |
3
|
pubmed:dateCreated |
1999-8-5
|
pubmed:abstractText |
Monoclonal antibodies were raised and selected against recombinant Plantago major PmSUC2 sucrose carrier protein. Epitopes of two monoclonal antibodies (PS2-1A2 and PS2-4D4) were mapped using N-terminally truncated PmSUC2 proteins and a lambda library displaying random PmSUC2 peptides. PS2-1A2 recognizes an octapeptide close to the N-terminus of PmSUC2, PS2-4D4 binds to a decapeptide at the very C-terminus. Analyses of antibody binding to yeast protoplasts with functionally active, tagged PmSUC2 protein revealed that both epitopes are located in cytoplasmic domains of PmSUC2. These results support a model for plant sucrose transporters containing 12 transmembrane helices with the N-terminus and the C-terminus on the cytoplasmic side of the plasma membrane.
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
Jun
|
pubmed:issn |
0014-5793
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:day |
25
|
pubmed:volume |
453
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
375-9
|
pubmed:dateRevised |
2006-11-15
|
pubmed:meshHeading |
pubmed-meshheading:10405179-Amino Acid Sequence,
pubmed-meshheading:10405179-Antibodies, Monoclonal,
pubmed-meshheading:10405179-Antibody Specificity,
pubmed-meshheading:10405179-Bacteriophage lambda,
pubmed-meshheading:10405179-Biological Transport,
pubmed-meshheading:10405179-Carrier Proteins,
pubmed-meshheading:10405179-Cell Membrane,
pubmed-meshheading:10405179-Cell Polarity,
pubmed-meshheading:10405179-Cytoplasm,
pubmed-meshheading:10405179-Epitope Mapping,
pubmed-meshheading:10405179-Membrane Transport Proteins,
pubmed-meshheading:10405179-Molecular Sequence Data,
pubmed-meshheading:10405179-Peptide Library,
pubmed-meshheading:10405179-Plant Proteins,
pubmed-meshheading:10405179-Plantago,
pubmed-meshheading:10405179-Plants, Medicinal,
pubmed-meshheading:10405179-Protein Conformation,
pubmed-meshheading:10405179-Recombinant Proteins,
pubmed-meshheading:10405179-Sucrose
|
pubmed:year |
1999
|
pubmed:articleTitle |
Structural analysis of a plant sucrose carrier using monoclonal antibodies and bacteriophage lambda surface display.
|
pubmed:affiliation |
Lehrstuhl Botanik II, Molekulare Pflanzenphysiologie, Universität Erlangen-Nürnberg, Erlangen, Germany.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|