| pubmed-article:9459306 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9459306 | lifeskim:mentions | umls-concept:C0015576 | lld:lifeskim |
| pubmed-article:9459306 | lifeskim:mentions | umls-concept:C0205474 | lld:lifeskim |
| pubmed-article:9459306 | lifeskim:mentions | umls-concept:C0074312 | lld:lifeskim |
| pubmed-article:9459306 | lifeskim:mentions | umls-concept:C1516771 | lld:lifeskim |
| pubmed-article:9459306 | lifeskim:mentions | umls-concept:C0597427 | lld:lifeskim |
| pubmed-article:9459306 | pubmed:issue | 2-3 | lld:pubmed |
| pubmed-article:9459306 | pubmed:dateCreated | 1998-2-27 | lld:pubmed |
| pubmed-article:9459306 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9459306 | pubmed:abstractText | HSP-3 is a member of the cysteine-rich secretory protein (CRISP) family from stallion seminal plasma. We report a large-scale purification protocol for native HSP-3. This protein is a non-glycosylated polypeptide chain with a pI of 8-9 and an isotope-averaged molecular mass of 24987 +/- 3 Da. The molecular mass of HSP-3, determined by equilibrium sedimentation, is 26 kDa, showing that the protein exists in solution as a monomer. The concentration of HSP-3 in the seminal plasma of different stallions ranged from 0.3 to 1.3 mg/ml. On average, 0.9-9 million HSP-3 molecules/cell coat the postacrosomal and mid-piece regions of an ejaculated, washed stallion spermatozoon, suggesting a role in sperm physiology. Conformational characterisation of purified HSP-3 was assessed by combination of circular dichroism and Fourier-transform infrared spectroscopies and differential scanning microcalorimetry. Based on secondary structure assignment, HSP-3 may belong to the alpha+beta class of proteins. Thermal denaturation of HSP-3 is irreversible and follows a non-two state transition characterised by a Tm of 64 degrees C, an enthalpy change of 75 kcal/mol, and a van 't Hoff enthalpy of 184 kcal/mol. Analysis of the spectroscopic and calorimetric data indicates the occurrence of aggregation of denatured HSP-3 molecules and suggests the monomer as the cooperative unfolding unit. | lld:pubmed |
| pubmed-article:9459306 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9459306 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9459306 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:9459306 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9459306 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9459306 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9459306 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9459306 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9459306 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:9459306 | pubmed:issn | 0014-5793 | lld:pubmed |
| pubmed-article:9459306 | pubmed:author | pubmed-author:UrbankeCC | lld:pubmed |
| pubmed-article:9459306 | pubmed:author | pubmed-author:GasserCC | lld:pubmed |
| pubmed-article:9459306 | pubmed:author | pubmed-author:Töpfer-Peters... | lld:pubmed |
| pubmed-article:9459306 | pubmed:author | pubmed-author:CalveteJ JJJ | lld:pubmed |
| pubmed-article:9459306 | pubmed:author | pubmed-author:VareaJJ | lld:pubmed |
| pubmed-article:9459306 | pubmed:author | pubmed-author:RaidaMM | lld:pubmed |
| pubmed-article:9459306 | pubmed:author | pubmed-author:MagdalenoLL | lld:pubmed |
| pubmed-article:9459306 | pubmed:author | pubmed-author:SchambonyA... | lld:pubmed |
| pubmed-article:9459306 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9459306 | pubmed:day | 29 | lld:pubmed |
| pubmed-article:9459306 | pubmed:volume | 420 | lld:pubmed |
| pubmed-article:9459306 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9459306 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9459306 | pubmed:pagination | 179-85 | lld:pubmed |
| pubmed-article:9459306 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:9459306 | pubmed:meshHeading | pubmed-meshheading:9459306-... | lld:pubmed |
| pubmed-article:9459306 | pubmed:meshHeading | pubmed-meshheading:9459306-... | lld:pubmed |
| pubmed-article:9459306 | pubmed:meshHeading | pubmed-meshheading:9459306-... | lld:pubmed |
| pubmed-article:9459306 | pubmed:meshHeading | pubmed-meshheading:9459306-... | lld:pubmed |
| pubmed-article:9459306 | pubmed:meshHeading | pubmed-meshheading:9459306-... | lld:pubmed |
| pubmed-article:9459306 | pubmed:meshHeading | pubmed-meshheading:9459306-... | lld:pubmed |
| pubmed-article:9459306 | pubmed:meshHeading | pubmed-meshheading:9459306-... | lld:pubmed |
| pubmed-article:9459306 | pubmed:meshHeading | pubmed-meshheading:9459306-... | lld:pubmed |
| pubmed-article:9459306 | pubmed:meshHeading | pubmed-meshheading:9459306-... | lld:pubmed |
| pubmed-article:9459306 | pubmed:meshHeading | pubmed-meshheading:9459306-... | lld:pubmed |
| pubmed-article:9459306 | pubmed:meshHeading | pubmed-meshheading:9459306-... | lld:pubmed |
| pubmed-article:9459306 | pubmed:meshHeading | pubmed-meshheading:9459306-... | lld:pubmed |
| pubmed-article:9459306 | pubmed:meshHeading | pubmed-meshheading:9459306-... | lld:pubmed |
| pubmed-article:9459306 | pubmed:meshHeading | pubmed-meshheading:9459306-... | lld:pubmed |
| pubmed-article:9459306 | pubmed:meshHeading | pubmed-meshheading:9459306-... | lld:pubmed |
| pubmed-article:9459306 | pubmed:meshHeading | pubmed-meshheading:9459306-... | lld:pubmed |
| pubmed-article:9459306 | pubmed:meshHeading | pubmed-meshheading:9459306-... | lld:pubmed |
| pubmed-article:9459306 | pubmed:meshHeading | pubmed-meshheading:9459306-... | lld:pubmed |
| pubmed-article:9459306 | pubmed:meshHeading | pubmed-meshheading:9459306-... | lld:pubmed |
| pubmed-article:9459306 | pubmed:meshHeading | pubmed-meshheading:9459306-... | lld:pubmed |
| pubmed-article:9459306 | pubmed:meshHeading | pubmed-meshheading:9459306-... | lld:pubmed |
| pubmed-article:9459306 | pubmed:meshHeading | pubmed-meshheading:9459306-... | lld:pubmed |
| pubmed-article:9459306 | pubmed:year | 1997 | lld:pubmed |
| pubmed-article:9459306 | pubmed:articleTitle | Biochemical and conformational characterisation of HSP-3, a stallion seminal plasma protein of the cysteine-rich secretory protein (CRISP) family. | lld:pubmed |
| pubmed-article:9459306 | pubmed:affiliation | Instituto de Química-Física Rocasolano, C.S.I.C., Madrid, Spain. | lld:pubmed |
| pubmed-article:9459306 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9459306 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:100033965 | entrezgene:pubmed | pubmed-article:9459306 | lld:entrezgene |
