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Purification and Partial Characterization of Milk Clotting Proteases from Flowers of Cynara cardunculus
Biotechnology ETH-Hönggerberg CH-8093 Zürich, Switzerland .ORCID iD: 0000-0001-8899-5046
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1990 (English)In: Phytochemistry, ISSN 0031-9422, E-ISSN 1873-3700, Vol. 29, no 5, p. 1405-1410Article in journal (Refereed) Published
Abstract [en]

Three proteases (cynarases 1, 2 and 3) with milk-clotting activity have been purified from dried flowers of Cynara cardunculus. The proteases are each composed of one large and one small subunit. The native Mr of the dimeric proteins is 49 000. The three proteases are glycoproteins containing N-linked high mannose type glycans. Cynarase 3 shows the highest proteolytic and milk-clotting activity. All three enzymes express maximum activity at pH 5.1. Inhibitor studies indicate that the cynarases are of the aspartic acid type. Antibodies raised against the large subunit of cynarase 3 cross-reacts with the large subunits of the other two cynarases after destruction of the glycan structure by periodate oxidation. 

Place, publisher, year, edition, pages
1990. Vol. 29, no 5, p. 1405-1410
National Category
Biochemistry and Molecular Biology
Research subject
Natural Science, Biochemistry
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URN: urn:nbn:se:lnu:diva-579DOI: 10.1016/0031-9422(90)80090-4OAI: oai:DiVA.org:lnu-579DiVA, id: diva2:307309
Available from: 2010-04-01 Created: 2010-04-01 Last updated: 2017-12-12Bibliographically approved

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Brodelius, Peter

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