PMID- 16130275
OWN - NLM
STAT- MEDLINE
DCOM- 20050926
LR  - 20190922
IS  - 0105-6263 (Print)
IS  - 0105-6263 (Linking)
VI  - 20
IP  - 5
DP  - 1997 Oct
TI  - Purification and characterization of hepatocyte growth factor (HGF) from human 
      seminal plasma.
PG  - 306-14
AB  - Naturally occurring forms of hepatocyte growth factor/scatter factor (HGF/SF) 
      have been purified by heparin-Sepharose chromatography, followed by cation 
      exchange chromatography from a pool of human seminal plasma. Using an 
      enzyme-linked immunosorbant assay, MDCK scatter assay, and Western blot analysis, 
      it was found that, after heparin-Sepharose chromatography, human HGF/SF present 
      in seminal plasma eluted in two different fractions, between 0.72 and 0.85 M NaCl 
      (fraction I) and between 0.95 and 1.10 M NaCl (fraction II). Further purification 
      of fraction I by cation exchange chromatography resulted again in two fractions 
      which eluted at 0.2-0.4 and at 0.6-0.8 M NaCl. The fraction which eluted at 
      0.2-0.4 M NaCl consisted of two biologically less active heavy chains of the 
      heterodimeric form of HGF/SF (107.1 U/ng immunoreactive HGF), with approximate 
      molecular weights of 65 and 62 kDa under reducing conditions. The second 
      fraction, which eluted at 0.6-0.8 M NaCl, revealed three bands with molecular 
      weights of 87, 65 and 62 kDa, respectively. The 87 kDa form is thought to be a 
      single chain precursor of HGF/SF devoid of biological activity. After subjecting 
      fraction II to cation exchange chromatography, only one major peak eluted between 
      0.9 and 1.0 M NaCl, and consisted of two biologically active heavy chains of the 
      heterodimeric form of HGF/SF (708.3 U/ng immunoreactive HGF), with approximate 
      molecular weights of 65 and 62 kDa under reducing conditions. Nonreducing 
      conditions for both fraction I and fraction II revealed only one band with a 
      molecular weight of 68 kDa. The ratio ofpro-HGF/SF and less biologically active 
      HGF/ SF (fraction I) over mature heterodimeric HGF/SF (fraction II) was 
      approximately 1:3, in seminal plasma from sperm donors. In seminal plasma, 
      pro-HGF/SF represents an 87 kDa glycoprotein which, apparently, is converted by 
      limited proteolysis into several bands with molecular weights of 65 and 62 kDa. 
      This is the first report showing the presence of pro-HGF/SF and heterodimeric 
      mature HGF/SF, as well as less biologically active forms of HGF/SF in human 
      seminal plasma.
FAU - Depuydt, C E
AU  - Depuydt CE
AD  - University Hospital Ghent, Department of Internal Medicne, Belgium.
FAU - Zalata, A
AU  - Zalata A
FAU - Falmagne, J B
AU  - Falmagne JB
FAU - Bosmans, E
AU  - Bosmans E
FAU - Comhaire, F H
AU  - Comhaire FH
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - Int J Androl
JT  - International journal of andrology
JID - 8000141
RN  - 67256-21-7 (Hepatocyte Growth Factor)
SB  - IM
MH  - Adult
MH  - Animals
MH  - Blotting, Western
MH  - Cells, Cultured
MH  - Chromatography, Affinity
MH  - Chromatography, Ion Exchange
MH  - Dogs
MH  - Electrophoresis, Polyacrylamide Gel
MH  - Hepatocyte Growth Factor/chemistry/*isolation & purification
MH  - Humans
MH  - Semen/*chemistry
EDAT- 2005/09/01 09:00
MHDA- 2005/09/27 09:00
CRDT- 2005/09/01 09:00
PHST- 2005/09/01 09:00 [pubmed]
PHST- 2005/09/27 09:00 [medline]
PHST- 2005/09/01 09:00 [entrez]
AID - 10.1046/j.1365-2605.1997.00074.x [doi]
PST - ppublish
SO  - Int J Androl. 1997 Oct;20(5):306-14. doi: 10.1046/j.1365-2605.1997.00074.x.