Article (Scientific journals)
Purification of Progelatinases A and B by Continuous-Elution Electrophoresis
Remacle, A. G.; Baramova, Eugéenia N.; Weidle, U. H. et al.
1995In Protein Expression and Purification, 6 (4), p. 417-22
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Abstract :
[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).
Disciplines :
Biochemistry, biophysics & molecular biology
Author, co-author :
Remacle, A. G.
Baramova, Eugéenia N.
Weidle, U. H.
Krell, H. W.
Foidart, Jean-Michel ;  Université de Liège - ULiège > Département des sciences cliniques > Gynécologie - Obstétrique - Labo de biologie des tumeurs et du développement
Language :
English
Title :
Purification of Progelatinases A and B by Continuous-Elution Electrophoresis
Publication date :
August 1995
Journal title :
Protein Expression and Purification
ISSN :
1046-5928
eISSN :
1096-0279
Publisher :
Academic Press, Orlando, United States - Florida
Volume :
6
Issue :
4
Pages :
417-22
Peer reviewed :
Peer Reviewed verified by ORBi
Available on ORBi :
since 26 January 2011

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