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Purification of DD-carboxypeptidases from Streptomyces strains R61 and K15 by antigen-antibody affinity chromatography
Marquet, A; Nguyen-Distèche, Martine; Leyh-Bouille, Mélina et al.
1978In Hoffmann-Ostenhof, Otto (Ed.) Affinity chromatography : biospecific sorption, the first extensive compendium on affinity chromatography as applied to biochemistry and immunochemistry
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Keywords :
purification; DD; carboxypeptidases; streptomyces; strains; R61; K15; antigen; antibody; affinity; chromatography
Abstract :
[en] The exocellular R61 DD-carboxypeptidase and the lysozyme-releasable K15 DD-carboxypeptidase were purified using anti-exocellular R61 enzyme IgG-Sepharose as immunoadsorbent. The specific activity of R61 enzyme was increased 70 fold (yield 90%) and that of K15 enzyme was increased 550 fold (yield 50% of the absorbed material).
Disciplines :
Biochemistry, biophysics & molecular biology
Author, co-author :
Marquet, A
Nguyen-Distèche, Martine ;  Université de Liège > Centre d'ingénierie des protéines
Leyh-Bouille, Mélina
Ghuysen, Jean-Marie ;  Université de Liège - ULiège > Centre d'Ingéniérie des Protéines
Language :
English
Title :
Purification of DD-carboxypeptidases from Streptomyces strains R61 and K15 by antigen-antibody affinity chromatography
Publication date :
1978
Main work title :
Affinity chromatography : biospecific sorption, the first extensive compendium on affinity chromatography as applied to biochemistry and immunochemistry
Editor :
Hoffmann-Ostenhof, Otto
Publisher :
Elsevier
ISBN/EAN :
0080226329
Pages :
251-255
Peer reviewed :
Peer reviewed
Available on ORBi :
since 20 March 2017

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