Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
2-3
|
| pubmed:dateCreated |
1998-2-27
|
| pubmed:databankReference | |
| 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.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Dec
|
| pubmed:issn |
0014-5793
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
29
|
| pubmed:volume |
420
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
179-85
|
| pubmed:dateRevised |
2006-11-15
|
| pubmed:meshHeading |
pubmed-meshheading:9459306-Animals,
pubmed-meshheading:9459306-Calorimetry, Differential Scanning,
pubmed-meshheading:9459306-Chromatography, Gel,
pubmed-meshheading:9459306-Circular Dichroism,
pubmed-meshheading:9459306-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:9459306-Fluorescent Antibody Technique,
pubmed-meshheading:9459306-Horses,
pubmed-meshheading:9459306-Isoelectric Point,
pubmed-meshheading:9459306-Male,
pubmed-meshheading:9459306-Mass Spectrometry,
pubmed-meshheading:9459306-Molecular Weight,
pubmed-meshheading:9459306-Prostatic Secretory Proteins,
pubmed-meshheading:9459306-Protein Conformation,
pubmed-meshheading:9459306-Protein Denaturation,
pubmed-meshheading:9459306-Protein Folding,
pubmed-meshheading:9459306-Protein Structure, Secondary,
pubmed-meshheading:9459306-Proteins,
pubmed-meshheading:9459306-Seminal Plasma Proteins,
pubmed-meshheading:9459306-Spectroscopy, Fourier Transform Infrared,
pubmed-meshheading:9459306-Spermatozoa,
pubmed-meshheading:9459306-Temperature,
pubmed-meshheading:9459306-Thermodynamics
|
| pubmed:year |
1997
|
| pubmed:articleTitle |
Biochemical and conformational characterisation of HSP-3, a stallion seminal plasma protein of the cysteine-rich secretory protein (CRISP) family.
|
| pubmed:affiliation |
Instituto de Química-Física Rocasolano, C.S.I.C., Madrid, Spain.
|
| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|