Reference : Purification of Progelatinases A and B by Continuous-Elution Electrophoresis
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/82888
Purification of Progelatinases A and B by Continuous-Elution Electrophoresis
English
Remacle, A. G. [> > > >]
Baramova, E. N. [> > > >]
Weidle, U. H. [> > > >]
Krell, H. W. [> > > >]
Foidart, Jean-Michel mailto [Université de Liège - ULg > Département des sciences cliniques > Gynécologie - Obstétrique - Labo de biologie des tumeurs et du développement >]
Aug-1995
Protein Expression & Purification
Academic Press
6
4
417-22
Yes (verified by ORBi)
International
1046-5928
1096-0279
Orlando
FL
[en] Progelatinases A and B were purified from HT1080-conditioned culture medium using a continuous-elution electrophoresis. Initially cell culture medium was ammonium sulfate precipitated. The concentrated proteins were affinity chromatographed on gelatin-Sepharose column. The bound gelatinases were eluted with electrophoresis sample buffer and subjected to continuous-elution electrophoresis. In a single run, under the standardized working conditions, the obtained fractions contained four purified enzymes--progelatinase A (M(r) 72,000), its activated forms (M(r) 62,000 and M(r) 59,000), and progelatinase B (M(r) 92,000). Moreover, the continuous-elution electrophoresis allowed the enzymes separation from their respective inhibitors--TIMP-1 (M(r) 28,500) and TIMP-2 (M(r) 21,000). The purified progelatinases A and B demonstrated high specific activities (150-200 U/micrograms).
http://hdl.handle.net/2268/82888
10.1006/prep.1995.1056

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