Purification and Partial Characterization of Milk Clotting Proteases from Flowers of Cynara cardunculus

Heimgartner, U (author)

Pietrzak, M (author)

Geertsen, R (author)

Brodelius, Peter (author): Biotechnology ETH-Hönggerberg CH-8093 Zürich, Switzerland

da Silva Figueiredo, A C (author)

S Pais, Maria (author)

(creator_code:org_t)

Elsevier BV, 1990
1990
English.
In: Phytochemistry. - : Elsevier BV. - 0031-9422 .- 1873-3700. ; 29:5, s. 1405-1410

Related links:: http://www.sciencedi...; show more...; https://urn.kb.se/re...; https://doi.org/10.1...; show less...

Abstract Subject headings

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.

By the author/editor: Heimgartner, U; Pietrzak, M; Geertsen, R; Brodelius, Peter; da Silva Figueir ...; S Pais, Maria

About the subject

NATURAL SCIENCES: NATURAL SCIENCES; and Biological Scien ...; and Biochemistry and ...

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