| pubmed-article:8724363 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8724363 | lifeskim:mentions | umls-concept:C0037868 | lld:lifeskim |
| pubmed-article:8724363 | lifeskim:mentions | umls-concept:C0923800 | lld:lifeskim |
| pubmed-article:8724363 | lifeskim:mentions | umls-concept:C0083996 | lld:lifeskim |
| pubmed-article:8724363 | lifeskim:mentions | umls-concept:C1749467 | lld:lifeskim |
| pubmed-article:8724363 | lifeskim:mentions | umls-concept:C0020197 | lld:lifeskim |
| pubmed-article:8724363 | pubmed:issue | 6 | lld:pubmed |
| pubmed-article:8724363 | pubmed:dateCreated | 1996-11-27 | lld:pubmed |
| pubmed-article:8724363 | pubmed:abstractText | The sperm plasma membrane protein PH-20 has a hyaluronidase activity that enables acrosome-intact sperm to pass through the cumulus cell layer of the egg. In this study we analyzed the relationship of guinea pig PH-20 and the "classical" soluble hyaluronidase released at the time of the acrosome reaction of guinea pig sperm. PH-20 is a membrane protein, anchored in the plasma and inner acrosomal membranes by a glycosyl phosphatidyl inositol anchor. Several types of experiments indicate a structural relationship of PH-20 and the soluble hyaluronidase released during the acrosome reaction. First, an antiserum raised against purified PH-20 is positive in an immunoblot of the soluble protein fraction released during the acrosome reaction. In the released, soluble protein fraction, the anti-PH-20 antiserum recognizes a protein of approximately 64 kDa, i.e., identical in molecular mass to PH-20 (approximately 64 kDa). Second, the enzymatic activity of the released hyaluronidase is completely inhibited (100%) by the anti-PH-20 antiserum. Third, almost all (97%) of the soluble hyaluronidase is removed from the released protein fraction by a single pass through an affinity column made with an anti-PH-20 monoclonal antibody. These findings suggest that the released, soluble hyaluronidase is a soluble form of PH-20 (sPH-20). During the acrosome reaction, PH-20 undergoes endoproteolytic cleavage into two disulfide-linked fragments whereas the released sPH-20 is not cleaved, suggesting the possible activity of a membrane-bound endoprotease on PH-20. We searched for a cDNA encoding sPH-20 but none was found. This result suggests that sPH-20 may arise from the enzymatic release of PH-20 from its membrane anchor, possibly at the time of acrosome reaction. | lld:pubmed |
| pubmed-article:8724363 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8724363 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8724363 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8724363 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8724363 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8724363 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8724363 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8724363 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8724363 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8724363 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8724363 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8724363 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:8724363 | pubmed:issn | 0006-3363 | lld:pubmed |
| pubmed-article:8724363 | pubmed:author | pubmed-author:PrimakoffPP | lld:pubmed |
| pubmed-article:8724363 | pubmed:author | pubmed-author:MylesD GDG | lld:pubmed |
| pubmed-article:8724363 | pubmed:author | pubmed-author:RamaraoC SCS | lld:pubmed |
| pubmed-article:8724363 | pubmed:author | pubmed-author:MahanKK | lld:pubmed |
| pubmed-article:8724363 | pubmed:author | pubmed-author:HunnicuttG... | lld:pubmed |
| pubmed-article:8724363 | pubmed:author | pubmed-author:LathropW FWF | lld:pubmed |
| pubmed-article:8724363 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8724363 | pubmed:volume | 54 | lld:pubmed |
| pubmed-article:8724363 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8724363 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8724363 | pubmed:pagination | 1343-9 | lld:pubmed |
| pubmed-article:8724363 | pubmed:dateRevised | 2010-4-1 | lld:pubmed |
| pubmed-article:8724363 | pubmed:meshHeading | pubmed-meshheading:8724363-... | lld:pubmed |
| pubmed-article:8724363 | pubmed:meshHeading | pubmed-meshheading:8724363-... | lld:pubmed |
| pubmed-article:8724363 | pubmed:meshHeading | pubmed-meshheading:8724363-... | lld:pubmed |
| pubmed-article:8724363 | pubmed:meshHeading | pubmed-meshheading:8724363-... | lld:pubmed |
| pubmed-article:8724363 | pubmed:meshHeading | pubmed-meshheading:8724363-... | lld:pubmed |
| pubmed-article:8724363 | pubmed:meshHeading | pubmed-meshheading:8724363-... | lld:pubmed |
| pubmed-article:8724363 | pubmed:meshHeading | pubmed-meshheading:8724363-... | lld:pubmed |
| pubmed-article:8724363 | pubmed:meshHeading | pubmed-meshheading:8724363-... | lld:pubmed |
| pubmed-article:8724363 | pubmed:meshHeading | pubmed-meshheading:8724363-... | lld:pubmed |
| pubmed-article:8724363 | pubmed:meshHeading | pubmed-meshheading:8724363-... | lld:pubmed |
| pubmed-article:8724363 | pubmed:meshHeading | pubmed-meshheading:8724363-... | lld:pubmed |
| pubmed-article:8724363 | pubmed:meshHeading | pubmed-meshheading:8724363-... | lld:pubmed |
| pubmed-article:8724363 | pubmed:meshHeading | pubmed-meshheading:8724363-... | lld:pubmed |
| pubmed-article:8724363 | pubmed:year | 1996 | lld:pubmed |
| pubmed-article:8724363 | pubmed:articleTitle | Structural relationship of sperm soluble hyaluronidase to the sperm membrane protein PH-20. | lld:pubmed |
| pubmed-article:8724363 | pubmed:affiliation | Department of Physiology, University of Connecticut Health Center, Farmington 06030, USA. | lld:pubmed |
| pubmed-article:8724363 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8724363 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:8724363 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:8724363 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:8724363 | lld:pubmed |
