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Lipoxygenase from peas, purification and properties of the enzyme
SIK – Svenska institutet för konserveringsforskning.
1970 (English)In: BBA - Enzymology, ISSN 0005-2744, Vol. 198, no 3, 449-459 p.Article in journal (Refereed)
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.

Place, publisher, year, edition, pages
1970. Vol. 198, no 3, 449-459 p.
Keyword [en]
Food Engineering
Keyword [sv]
Livsmedelsteknik
National Category
Food Science
Identifiers
URN: urn:nbn:se:ri:diva-8378DOI: 10.1016/0005-2744(70)90123-3PubMedID: 5436155OAI: oai:DiVA.org:ri-8378DiVA: diva2:966249
Available from: 2016-09-08 Created: 2016-09-08Bibliographically approved

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SIK – Svenska institutet för konserveringsforskning
Food Science

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