pubmed-article:3480243 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:3480243 | lifeskim:mentions | umls-concept:C0019360 | lld:lifeskim |
pubmed-article:3480243 | lifeskim:mentions | umls-concept:C0001214 | lld:lifeskim |
pubmed-article:3480243 | lifeskim:mentions | umls-concept:C0036734 | lld:lifeskim |
pubmed-article:3480243 | lifeskim:mentions | umls-concept:C2717971 | lld:lifeskim |
pubmed-article:3480243 | lifeskim:mentions | umls-concept:C1323247 | lld:lifeskim |
pubmed-article:3480243 | lifeskim:mentions | umls-concept:C0679622 | lld:lifeskim |
pubmed-article:3480243 | lifeskim:mentions | umls-concept:C0205314 | lld:lifeskim |
pubmed-article:3480243 | lifeskim:mentions | umls-concept:C0871161 | lld:lifeskim |
pubmed-article:3480243 | pubmed:issue | 1 | lld:pubmed |
pubmed-article:3480243 | pubmed:dateCreated | 1988-1-27 | lld:pubmed |
pubmed-article:3480243 | pubmed:abstractText | The major fucose-binding protein of 53 kDa from boar spermatozoa was isolated to apparent homogeneity using a two-step procedure including high-performance gel filtration and reversed-phase chromatography. The N-terminal sequence of the protein revealed that it is identical with the sperm proteinase acrosin. By means of a solid-phase zona-binding assay based on the avidin-biotin system it was demonstrated that acrosin also interacts strongly with porcine zona pellucida. Thus, the acrosin molecule combines specific proteolytic activity with zona- and carbohydrate-affinity properties, i.e. previously unrecognized properties of a serine proteinase. It seems likely that this special affinity of acrosin directs the proteolytic activity to its structural target in the vivo situation. | lld:pubmed |
pubmed-article:3480243 | pubmed:language | eng | lld:pubmed |
pubmed-article:3480243 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3480243 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:3480243 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3480243 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3480243 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3480243 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:3480243 | pubmed:month | Dec | lld:pubmed |
pubmed-article:3480243 | pubmed:issn | 0014-5793 | lld:pubmed |
pubmed-article:3480243 | pubmed:author | pubmed-author:HenschenAA | lld:pubmed |
pubmed-article:3480243 | pubmed:author | pubmed-author:Töpfer-Peters... | lld:pubmed |
pubmed-article:3480243 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:3480243 | pubmed:day | 21 | lld:pubmed |
pubmed-article:3480243 | pubmed:volume | 226 | lld:pubmed |
pubmed-article:3480243 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:3480243 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:3480243 | pubmed:pagination | 38-42 | lld:pubmed |
pubmed-article:3480243 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
pubmed-article:3480243 | pubmed:meshHeading | pubmed-meshheading:3480243-... | lld:pubmed |
pubmed-article:3480243 | pubmed:meshHeading | pubmed-meshheading:3480243-... | lld:pubmed |
pubmed-article:3480243 | pubmed:meshHeading | pubmed-meshheading:3480243-... | lld:pubmed |
pubmed-article:3480243 | pubmed:meshHeading | pubmed-meshheading:3480243-... | lld:pubmed |
pubmed-article:3480243 | pubmed:meshHeading | pubmed-meshheading:3480243-... | lld:pubmed |
pubmed-article:3480243 | pubmed:meshHeading | pubmed-meshheading:3480243-... | lld:pubmed |
pubmed-article:3480243 | pubmed:meshHeading | pubmed-meshheading:3480243-... | lld:pubmed |
pubmed-article:3480243 | pubmed:meshHeading | pubmed-meshheading:3480243-... | lld:pubmed |
pubmed-article:3480243 | pubmed:meshHeading | pubmed-meshheading:3480243-... | lld:pubmed |
pubmed-article:3480243 | pubmed:meshHeading | pubmed-meshheading:3480243-... | lld:pubmed |
pubmed-article:3480243 | pubmed:meshHeading | pubmed-meshheading:3480243-... | lld:pubmed |
pubmed-article:3480243 | pubmed:year | 1987 | lld:pubmed |
pubmed-article:3480243 | pubmed:articleTitle | Acrosin shows zona and fucose binding, novel properties for a serine proteinase. | lld:pubmed |
pubmed-article:3480243 | pubmed:affiliation | Department of Dermatology, University of Munich, FRG. | lld:pubmed |
pubmed-article:3480243 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:3480243 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
entrez-gene:397098 | entrezgene:pubmed | pubmed-article:3480243 | lld:entrezgene |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3480243 | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3480243 | lld:pubmed |