| pubmed-article:16493076 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16493076 | lifeskim:mentions | umls-concept:C0003250 | lld:lifeskim |
| pubmed-article:16493076 | lifeskim:mentions | umls-concept:C0001128 | lld:lifeskim |
| pubmed-article:16493076 | lifeskim:mentions | umls-concept:C0205177 | lld:lifeskim |
| pubmed-article:16493076 | lifeskim:mentions | umls-concept:C0656016 | lld:lifeskim |
| pubmed-article:16493076 | lifeskim:mentions | umls-concept:C1417635 | lld:lifeskim |
| pubmed-article:16493076 | lifeskim:mentions | umls-concept:C1420797 | lld:lifeskim |
| pubmed-article:16493076 | lifeskim:mentions | umls-concept:C0596973 | lld:lifeskim |
| pubmed-article:16493076 | lifeskim:mentions | umls-concept:C0376315 | lld:lifeskim |
| pubmed-article:16493076 | lifeskim:mentions | umls-concept:C1882074 | lld:lifeskim |
| pubmed-article:16493076 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:16493076 | lifeskim:mentions | umls-concept:C0205254 | lld:lifeskim |
| pubmed-article:16493076 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:16493076 | pubmed:dateCreated | 2006-2-22 | lld:pubmed |
| pubmed-article:16493076 | pubmed:abstractText | The novel tetrameric structure of human beta-tryptase faces each active site into the central pore, thereby restricting access of most biologic protease inhibitors. The mechanism by which the anti-tryptase mAb B12 inhibits human beta-tryptase peptidase and proteolytic activities at neutral pH, but augments proteolytic activity at acidic pH, was examined. At neutral pH, B12-beta-tryptase complexes are inactive. At acidic pH, B12 (intact and Fab) minimally affects peptidase activity when added to beta-tryptase tetramers, but does induce susceptibility to inhibition by soybean trypsin inhibitor and antithrombin III. Surprisingly, B12 Fab-beta-tryptase complexes formed at both neutral and acidic pH exhibit the apparent molecular mass of a complex with 1 beta-tryptase monomer and 1 Fab by gel filtration. B12 does not compete with heparin for binding to tryptase at either neutral or acidic pH. Thus, B12 directly disrupts beta-tryptase tetramers to monomers that are inactive at neutral pH, whereas at acidic pH, are active and more accessible to protein inhibitors and substrates. | lld:pubmed |
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| pubmed-article:16493076 | pubmed:language | eng | lld:pubmed |
| pubmed-article:16493076 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16493076 | pubmed:citationSubset | AIM | lld:pubmed |
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| pubmed-article:16493076 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16493076 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:16493076 | pubmed:issn | 0022-1767 | lld:pubmed |
| pubmed-article:16493076 | pubmed:author | pubmed-author:SchwartzLawre... | lld:pubmed |
| pubmed-article:16493076 | pubmed:author | pubmed-author:YoshihiroFuku... | lld:pubmed |
| pubmed-article:16493076 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:16493076 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:16493076 | pubmed:volume | 176 | lld:pubmed |
| pubmed-article:16493076 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16493076 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16493076 | pubmed:pagination | 3165-72 | lld:pubmed |
| pubmed-article:16493076 | pubmed:dateRevised | 2011-8-1 | lld:pubmed |
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| pubmed-article:16493076 | pubmed:year | 2006 | lld:pubmed |
| pubmed-article:16493076 | pubmed:articleTitle | The B12 anti-tryptase monoclonal antibody disrupts the tetrameric structure of heparin-stabilized beta-tryptase to form monomers that are inactive at neutral pH and active at acidic pH. | lld:pubmed |
| pubmed-article:16493076 | pubmed:affiliation | Division of Rheumatology, Allergy and Immunology, Department of Internal Medicine, Virginia Commonwealth University, Richmond, VA 23298, USA. | lld:pubmed |
| pubmed-article:16493076 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:16493076 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:16493076 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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