Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
19
|
| pubmed:dateCreated |
1993-7-27
|
| pubmed:abstractText |
Prekallikrein, a glycoprotein involved in contact phase activation, circulates in plasma in the form of a binary complex with high molecular weight kininogen (H-kininogen). The binding to H-kininogen is mediated by the prekallikrein heavy chain consisting of four repetitive domains, A1-A4. To define more precisely the region(s) involved in kininogen binding, we have employed an affinity cross-linking strategy with a synthetic peptide of 31 residues which mimics the prekallikrein binding site of H-kininogen. Cross-linking of the radiolabeled peptide to (pre)kallikrein revealed a binding segment in the NH2-terminal portion of the prekallikrein heavy chain; another binding segment was located in the COOH-terminal part of the heavy chain. The latter binding segment is harbored by a previously identified fragment of the kallikrein heavy chain involved in H-kininogen binding (Page, J.D., and Colman, R.W. (1991) J. Biol. Chem. 266, 8143-8148). Chemical cleavage of the heavy chain cross-linked with the radiolabeled peptide mapped the NH2-terminal binding segment to 60 residues (positions 53-112) of A1. Synthesis of a peptide (positions 56-86) and development of specific antibodies to this peptide narrowed down the kininogen binding segment to 31 residues of the center portion of A1. This NH2-terminal segment is equivalent to a kininogen binding site previously identified in factor XI (Baglia, F.A., Jameson, B.A., and Walsh, P.N. (1992) J. Biol. Chem. 267, 4247-4252). We conclude that prekallikrein exposes at least two segments on its heavy chain portion which form a continuous surface thereby facilitating the intimate binding of the zymogen to its nonenzymatic cofactor, H-kininogen.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Epitopes,
http://linkedlifedata.com/resource/pubmed/chemical/Iodine Radioisotopes,
http://linkedlifedata.com/resource/pubmed/chemical/Kininogens,
http://linkedlifedata.com/resource/pubmed/chemical/Macromolecular Substances,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/Prekallikrein
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Jul
|
| pubmed:issn |
0021-9258
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
5
|
| pubmed:volume |
268
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
14527-35
|
| pubmed:dateRevised |
2006-11-15
|
| pubmed:meshHeading |
pubmed-meshheading:7686159-Amino Acid Sequence,
pubmed-meshheading:7686159-Autoradiography,
pubmed-meshheading:7686159-Binding, Competitive,
pubmed-meshheading:7686159-Binding Sites,
pubmed-meshheading:7686159-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:7686159-Enzyme-Linked Immunosorbent Assay,
pubmed-meshheading:7686159-Epitopes,
pubmed-meshheading:7686159-Humans,
pubmed-meshheading:7686159-Iodine Radioisotopes,
pubmed-meshheading:7686159-Kinetics,
pubmed-meshheading:7686159-Kininogens,
pubmed-meshheading:7686159-Macromolecular Substances,
pubmed-meshheading:7686159-Models, Structural,
pubmed-meshheading:7686159-Molecular Sequence Data,
pubmed-meshheading:7686159-Molecular Weight,
pubmed-meshheading:7686159-Peptide Fragments,
pubmed-meshheading:7686159-Peptides,
pubmed-meshheading:7686159-Prekallikrein
|
| pubmed:year |
1993
|
| pubmed:articleTitle |
Mapping of the high molecular weight kininogen binding site of prekallikrein. Evidence for a discontinuous epitope formed by distinct segments of the prekallikrein heavy chain.
|
| pubmed:affiliation |
Institute for Physiological Chemistry and Pathobiochemistry, University of Mainz, Germany.
|
| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|