| pubmed-article:7685348 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7685348 | lifeskim:mentions | umls-concept:C0055857 | lld:lifeskim |
| pubmed-article:7685348 | lifeskim:mentions | umls-concept:C0205280 | lld:lifeskim |
| pubmed-article:7685348 | lifeskim:mentions | umls-concept:C0208531 | lld:lifeskim |
| pubmed-article:7685348 | pubmed:issue | 17 | lld:pubmed |
| pubmed-article:7685348 | pubmed:dateCreated | 1993-7-13 | lld:pubmed |
| pubmed-article:7685348 | pubmed:abstractText | F1-20 and AP-3 are independently described, synapse-associated, developmentally regulated phosphoproteins with similar apparent molecular masses on SDS-polyacrylamide gel electrophoresis (PAGE). F1-20 was cloned and characterized because of its synapse specificity. AP-3 was purified and studied biochemically because of its function as a clathrin assembly protein. Here we present evidence that establishes the identity of F1-20 and AP-3. Monoclonal antibodies against F1-20 and AP-3 both specifically recognize a single protein from mouse brain with an apparent molecular mass of 190 kDa on SDS-PAGE. These monoclonal antibodies also specifically recognize the cloned F1-20 protein expressed in Escherichia coli. The anti-F1-20 monoclonal antibody (mAb) stains a bovine protein with an apparent molecular mass on SDS-PAGE of 190 kDa that copurifies with brain clathrin-coated vesicles (CCVs) and that can be extracted from the brain CCVs under conditions that extract AP-3. The anti-F1-20 and anti-AP-3 mAbs specifically recognize the same spot on a two-dimensional gel run on a bovine brain clathrin-coated vesicle extract. AP-3 purified from bovine brain CCVs is recognized by both the anti-F1-20 and anti-AP-3 mAbs. Purified preparations of bovine AP-3 and bacterially expressed mouse F1-20 give identical patterns of protease digestion with bromelain and subtilisin. Sequence analyses reveal that F1-20 has an essentially neutral 30-kDa NH2-terminal domain with an amino acid composition typical of a globular structure and an acidic COOH-terminal domain rich in proline, serine, threonine, and alanine. This is consistent with proteolysis experiments that suggested that AP-3 could be divided into a 30-kDa globular uncharged clathrin-binding domain and an acidic, anomalously migrating domain. | lld:pubmed |
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| pubmed-article:7685348 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7685348 | pubmed:language | eng | lld:pubmed |
| pubmed-article:7685348 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7685348 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:7685348 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:7685348 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:7685348 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:7685348 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7685348 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7685348 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:7685348 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:7685348 | pubmed:author | pubmed-author:PuszkinSS | lld:pubmed |
| pubmed-article:7685348 | pubmed:author | pubmed-author:YangJJ | lld:pubmed |
| pubmed-article:7685348 | pubmed:author | pubmed-author:ZhouSS | lld:pubmed |
| pubmed-article:7685348 | pubmed:author | pubmed-author:LaferE MEM | lld:pubmed |
| pubmed-article:7685348 | pubmed:author | pubmed-author:TanneryN HNH | lld:pubmed |
| pubmed-article:7685348 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7685348 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:7685348 | pubmed:volume | 268 | lld:pubmed |
| pubmed-article:7685348 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7685348 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7685348 | pubmed:pagination | 12655-62 | lld:pubmed |
| pubmed-article:7685348 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:7685348 | pubmed:year | 1993 | lld:pubmed |
| pubmed-article:7685348 | pubmed:articleTitle | The synapse-specific phosphoprotein F1-20 is identical to the clathrin assembly protein AP-3. | lld:pubmed |
| pubmed-article:7685348 | pubmed:affiliation | Department of Biological Sciences, University of Pittsburgh, Pennsylvania 15260. | lld:pubmed |
| pubmed-article:7685348 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:7685348 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:7685348 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:7685348 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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