pubmed-article:1731778 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:1731778 | lifeskim:mentions | umls-concept:C0597357 | lld:lifeskim |
pubmed-article:1731778 | lifeskim:mentions | umls-concept:C1257739 | lld:lifeskim |
pubmed-article:1731778 | lifeskim:mentions | umls-concept:C1521761 | lld:lifeskim |
pubmed-article:1731778 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
pubmed-article:1731778 | pubmed:issue | 1 | lld:pubmed |
pubmed-article:1731778 | pubmed:dateCreated | 1992-2-18 | lld:pubmed |
pubmed-article:1731778 | pubmed:abstractText | Scatchard plot analysis of the binding of 125I-labeled heparin binding cell growth-associated factor (125I-HBGAF) to NIH 3T3 cells revealed a single class of high affinity receptors (-5000/cell) with kd of -0.6 nM. 125I-HBGAF was covalently cross-linked to the cell surface receptor on NIH 3T3 cells with disuccinimidyl suberate (DSS). Two 125I-HBGAF-cross-linked complexes of 170 kDa and 142 kDa were observed on SDS-polyacrylamide gel electrophoresis under reducing and nonreducing conditions. The 125I-HBGAF-cross-linked complex formation was completely abolished in the presence of greater than or equal to 100-fold excess of unlabeled HBGAF but not PDGF, EGF, aFGF, bFGF, or insulin. 125I-HBGAF appeared to undergo rapid internalization and relatively slow degradation following binding to the HBGAF receptor on NIH 3T3 cells. These results suggest that NIH 3T3 cells express a high affinity HBGAF receptor which shows two different estimated molecular masses of -155 kDa and -127 kDa. This high affinity HBGAF receptor was also found to express in other cell types. | lld:pubmed |
pubmed-article:1731778 | pubmed:language | eng | lld:pubmed |
pubmed-article:1731778 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1731778 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:1731778 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1731778 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1731778 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1731778 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1731778 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1731778 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1731778 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1731778 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1731778 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:1731778 | pubmed:month | Jan | lld:pubmed |
pubmed-article:1731778 | pubmed:issn | 0006-291X | lld:pubmed |
pubmed-article:1731778 | pubmed:author | pubmed-author:HuangJ SJS | lld:pubmed |
pubmed-article:1731778 | pubmed:author | pubmed-author:HuangS SSS | lld:pubmed |
pubmed-article:1731778 | pubmed:author | pubmed-author:KuoM DMD | lld:pubmed |
pubmed-article:1731778 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:1731778 | pubmed:day | 15 | lld:pubmed |
pubmed-article:1731778 | pubmed:volume | 182 | lld:pubmed |
pubmed-article:1731778 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:1731778 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:1731778 | pubmed:pagination | 188-94 | lld:pubmed |
pubmed-article:1731778 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
pubmed-article:1731778 | pubmed:meshHeading | pubmed-meshheading:1731778-... | lld:pubmed |
pubmed-article:1731778 | pubmed:meshHeading | pubmed-meshheading:1731778-... | lld:pubmed |
pubmed-article:1731778 | pubmed:meshHeading | pubmed-meshheading:1731778-... | lld:pubmed |
pubmed-article:1731778 | pubmed:meshHeading | pubmed-meshheading:1731778-... | lld:pubmed |
pubmed-article:1731778 | pubmed:meshHeading | pubmed-meshheading:1731778-... | lld:pubmed |
pubmed-article:1731778 | pubmed:meshHeading | pubmed-meshheading:1731778-... | lld:pubmed |
pubmed-article:1731778 | pubmed:meshHeading | pubmed-meshheading:1731778-... | lld:pubmed |
pubmed-article:1731778 | pubmed:meshHeading | pubmed-meshheading:1731778-... | lld:pubmed |
pubmed-article:1731778 | pubmed:meshHeading | pubmed-meshheading:1731778-... | lld:pubmed |
pubmed-article:1731778 | pubmed:meshHeading | pubmed-meshheading:1731778-... | lld:pubmed |
pubmed-article:1731778 | pubmed:meshHeading | pubmed-meshheading:1731778-... | lld:pubmed |
pubmed-article:1731778 | pubmed:meshHeading | pubmed-meshheading:1731778-... | lld:pubmed |
pubmed-article:1731778 | pubmed:meshHeading | pubmed-meshheading:1731778-... | lld:pubmed |
pubmed-article:1731778 | pubmed:meshHeading | pubmed-meshheading:1731778-... | lld:pubmed |
pubmed-article:1731778 | pubmed:year | 1992 | lld:pubmed |
pubmed-article:1731778 | pubmed:articleTitle | Characterization of heparin-binding growth-associated factor receptor on NIH 3T3 cells. | lld:pubmed |
pubmed-article:1731778 | pubmed:affiliation | Department of Biochemistry and Molecular Biology, St. Louis University School of Medicine, MO 63104. | lld:pubmed |
pubmed-article:1731778 | pubmed:publicationType | Journal Article | lld:pubmed |