pubmed-article:8624844 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:8624844 | lifeskim:mentions | umls-concept:C0039005 | lld:lifeskim |
pubmed-article:8624844 | lifeskim:mentions | umls-concept:C0018183 | lld:lifeskim |
pubmed-article:8624844 | lifeskim:mentions | umls-concept:C0006732 | lld:lifeskim |
pubmed-article:8624844 | lifeskim:mentions | umls-concept:C0054504 | lld:lifeskim |
pubmed-article:8624844 | lifeskim:mentions | umls-concept:C0439855 | lld:lifeskim |
pubmed-article:8624844 | lifeskim:mentions | umls-concept:C1879748 | lld:lifeskim |
pubmed-article:8624844 | lifeskim:mentions | umls-concept:C1706853 | lld:lifeskim |
pubmed-article:8624844 | pubmed:issue | 1 | lld:pubmed |
pubmed-article:8624844 | pubmed:dateCreated | 1996-6-24 | lld:pubmed |
pubmed-article:8624844 | pubmed:abstractText | Calgranulin A (CAGA) and calgranulin B (CAGB) are two S100-like calcium-binding proteins that in human, bovine and mouse granulocytes are associated into a heterocomplex. We have previously identified in pig granulocytes the porcine homologue of CAGA and a novel S100-like protein which was named calgranulin C (CAGC). As pig CAGA is not associated with CAGC, we herein investigate its possible association with other proteins. CAGA was purified from pig granulocytes by gel filtration followed by Mono Q chromatography. The purified fractions were analysed by SDS-polyacrylamide gel electrophoresis, isoelectric focusing, mass spectrometry, chemical cross-linking and hydrophobic interaction chromatography. The CAGA-associated protein was further characterized by amino acid sequencing. Two CAGA-containing fractions were isolated. One of them was identified as a CAGA homodimer. The other fraction consists of a heterocomplex containing CAGA and a pI 7.0 calcium-binding protein; this protein has a molecular mass of 15,877.9 +/- 3.8 Da (mean +/- SD) whereas it migrates on 10 and 16% polyacrylamide gels as a 24- and 20-kDa protein, respectively. The pI 7.0 protein was identified by internal amino acid sequencing as the porcine homologue of CAGB. The stoichiometry of the heterocomplex was estimated to be 1:1. Both the CAGA homodimer and CAGA/CAGB were found to be non-covalently associated. Unlike the homodimer, CAGA/CAGB was bound to a Phenyl Superose column in a calcium-dependent manner. Our results suggest that pig granulocytes contain, in addition to CAGC, a CAGA homodimer and a CAGA/CAGB heterodimer. It is proposed that CAGB/CAGB and the CAGA homodimer may play different roles in vivo. | lld:pubmed |
pubmed-article:8624844 | pubmed:language | eng | lld:pubmed |
pubmed-article:8624844 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8624844 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:8624844 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8624844 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8624844 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8624844 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8624844 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8624844 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:8624844 | pubmed:month | Jan | lld:pubmed |
pubmed-article:8624844 | pubmed:issn | 1357-2725 | lld:pubmed |
pubmed-article:8624844 | pubmed:author | pubmed-author:SimpsonR JRJ | lld:pubmed |
pubmed-article:8624844 | pubmed:author | pubmed-author:SantomeJ AJA | lld:pubmed |
pubmed-article:8624844 | pubmed:author | pubmed-author:Dell'Angelica... | lld:pubmed |
pubmed-article:8624844 | pubmed:author | pubmed-author:SchleicherC... | lld:pubmed |
pubmed-article:8624844 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:8624844 | pubmed:volume | 28 | lld:pubmed |
pubmed-article:8624844 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:8624844 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:8624844 | pubmed:pagination | 53-62 | lld:pubmed |
pubmed-article:8624844 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
pubmed-article:8624844 | pubmed:meshHeading | pubmed-meshheading:8624844-... | lld:pubmed |
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pubmed-article:8624844 | pubmed:year | 1996 | lld:pubmed |
pubmed-article:8624844 | pubmed:articleTitle | Complex assembly of calgranulins A and B, two S100-like calcium-binding proteins from pig granulocytes. | lld:pubmed |
pubmed-article:8624844 | pubmed:affiliation | Instituto de Quimica y Fisicoquímica Biológicas, Facultad de Farmacia y Bioquímica, Universidad de Buenos Aires, Argentina. | lld:pubmed |
pubmed-article:8624844 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:8624844 | pubmed:publicationType | Comparative Study | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:8624844 | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:8624844 | lld:pubmed |