Non-conventional affinity chromatography of serine proteinases and their inhibitors

• Autorzy: Polanowski A. , Wilimowska-Pelc A. , Kowalska J. , Grybel J. , Zelazko M. , Wilusz T.
• Języki publikacji: EN

Abstrakty

EN

From among a wide variety of protein purification techniques affinity chromatogra­phy has proved to be particularly effective for separation of proteolytic enzymes and their inhibitors. In this article, following a general description of affinity adsorbents used for purification of proteinases, we overview a simple separation procedure for some serine proteinases and their inhibitors by way of affinity chromatography in the presence of high NaCl concentration. It has been shown that some highly specific trypsin inhibitors exhibit also antichymotrypsin activity when high concentration of Na+ but not K+ or Li+ ions are present in the reaction mixture. Taking advantage of this phenomenon the virgin forms of trypsin inhibitors from squash seeds, Kazal-type inhibitor from porcine pancreas and arproteinase inhibitor from human and sheep plasma, as an example, were separated using immobilized chymotrypsin or its inac­tive derivative methylchymotrypsin in the presence of 5 M NaCl.

Słowa kluczowe

EN

proteolytic enzyme; affinity chromatography; alpha1-proteinase inhibitor; serine proteinase; chymotrypsin; chromatography; trypsin; Kazal-type inhibitor; inhibitor; protein synthesis

• Wydawca: -
• Czasopismo: Acta Biochimica Polonica
• Rocznik: 2003
• Tom: 50
• Numer: 3
• Opis fizyczny: p.765-773,fig.

Twórcy

autor

Polanowski A.

• University of Wroclaw, Tamka 2, 50-137 Wroclaw, Poland

autor

Wilimowska-Pelc A.

autor

Kowalska J.

autor

Grybel J.

autor

Zelazko M.

autor

Wilusz T.

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