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Lipoxygenase from peas, purification and properties of the enzyme
RISE., SP – Sveriges Tekniska Forskningsinstitut, SP Sveriges tekniska forskningsinstitut, SIK – Svenska institutet för konserveringsforskning.
1970 (engelsk)Inngår i: BBA - Enzymology, ISSN 0005-2744, Vol. 198, nr 3, s. 449-459Artikkel i tidsskrift (Fagfellevurdert)
Abstract [en]

1. 1. Lipoxygenase (linoleate:oxygen oxidoreductase, EC 1.13.1.13.) from peas was extensively purified by precipitation with (NH4)2SO4, gel filtration with Sephadex G-150, and ion-exchange chromatography on DEAE-cellulose. 2. 2. The final enzyme preparation proved homogeneous by ultracentrifugation of a 0.6% protein solution (pH 7.0) but separated into two main and narrow fractions on isoelectric focusing, pI values 5.80-5.82. 3. 3. The molecular weight, as calculated on the basis of amino acid analysis and ultracentrifugation, was found to be 72 000 and 67 000, respectively. 4. 4. Pea lipoxygenase contains 7 half-cystine residues, different from the soybean enzyme which has been reported to contain none. © 1970.

sted, utgiver, år, opplag, sider
1970. Vol. 198, nr 3, s. 449-459
Emneord [en]
Food Engineering
Emneord [sv]
Livsmedelsteknik
HSV kategori
Identifikatorer
URN: urn:nbn:se:ri:diva-8378DOI: 10.1016/0005-2744(70)90123-3PubMedID: 5436155OAI: oai:DiVA.org:ri-8378DiVA, id: diva2:966249
Tilgjengelig fra: 2016-09-08 Laget: 2016-09-08 Sist oppdatert: 2025-09-23bibliografisk kontrollert

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