Search: onr:"swepub:oai:DiVA.org:lnu-579" > Purification and Pa...
Fältnamn | Indikatorer | Metadata |
---|---|---|
000 | 02642naa a2200397 4500 | |
001 | oai:DiVA.org:lnu-579 | |
003 | SwePub | |
008 | 100401s1990 | |||||||||||000 ||eng| | |
024 | 7 | a https://urn.kb.se/resolve?urn=urn:nbn:se:lnu:diva-5792 URI |
024 | 7 | a https://doi.org/10.1016/0031-9422(90)80090-42 DOI |
040 | a (SwePub)lnu | |
041 | a engb eng | |
042 | 9 SwePub | |
072 | 7 | a ref2 swepub-contenttype |
072 | 7 | a art2 swepub-publicationtype |
100 | 1 | a Heimgartner, U4 aut |
245 | 1 0 | a Purification and Partial Characterization of Milk Clotting Proteases from Flowers of Cynara cardunculus |
264 | 1 | b Elsevier BV,c 1990 |
338 | a print2 rdacarrier | |
520 | a 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. | |
650 | 7 | a NATURVETENSKAPx Biologix Biokemi och molekylärbiologi0 (SwePub)106022 hsv//swe |
650 | 7 | a NATURAL SCIENCESx Biological Sciencesx Biochemistry and Molecular Biology0 (SwePub)106022 hsv//eng |
653 | a Biochemistry | |
653 | a Biokemi | |
653 | a Biochemistry | |
653 | a Biokemi | |
700 | 1 | a Pietrzak, M4 aut |
700 | 1 | a Geertsen, R4 aut |
700 | 1 | a Brodelius, Peteru Biotechnology ETH-Hönggerberg CH-8093 Zürich, Switzerland4 aut0 (Swepub:lnu)nbrpe |
700 | 1 | a da Silva Figueiredo, A C4 aut |
700 | 1 | a S Pais, Maria4 aut |
710 | 2 | a Biotechnology ETH-Hönggerberg CH-8093 Zürich, Switzerland4 org |
773 | 0 | t Phytochemistryd : Elsevier BVg 29:5, s. 1405-1410q 29:5<1405-1410x 0031-9422x 1873-3700 |
856 | 4 | u http://www.sciencedirect.com/science?_ob=ArticleURL&_aset=V-WA-A-W-D-MsSAYVA-UUW-U-AACVBCZUAE-AACAEBZYAE-EDVZDDADU-D-U&_rdoc=4&_fmt=summary&_udi=B6TH7-42K6D2S-D0&_coverDate=12%2F31%2F1990&_cdi=5275&_orig=search&_st=13&_sort=d&view=c&_acct=C000050221&_version=1&_urlVersion=0&_userid=10&md5=024b02f5245b9a6e791c15290d23d230y Länktext |
856 | 4 8 | u https://urn.kb.se/resolve?urn=urn:nbn:se:lnu:diva-579 |
856 | 4 8 | u https://doi.org/10.1016/0031-9422(90)80090-4 |
Kungliga biblioteket hanterar dina personuppgifter i enlighet med EU:s dataskyddsförordning (2018), GDPR. Läs mer om hur det funkar här.
Så här hanterar KB dina uppgifter vid användning av denna tjänst.