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- Watanabe, A, et al.
(författare)
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Gunnar Fant 60 years
- 1979
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Ingår i: TMH-QPSR. ; 20:2, s. 1-45
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Tidskriftsartikel (refereegranskat)
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| 2. |
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| 3. |
- Eriksson, Caj, et al.
(författare)
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Denatured hemoproteins as catalysts in lipid oxidation
- 1971
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Ingår i: Journal of the American Oil Chemists Society. - 0003-021X .- 1558-9331. ; 48:9, s. 442-447
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Tidskriftsartikel (refereegranskat)abstract
- Purified catalase and peroxidase were denatured by heat, acid and urea. Denaturation resulted in up to 22-fold increase in nonenzymatic lipid oxidation activity concomitant with loss of enzymatic activity. It is proposed that the increased nonenzymatic activity is due to increased exposure of the heme group. Acid-splitting of the hemoproteins into apoprotein and hemin had the greatest influence on both of the catalytic activities and recombination reversed the effect. Urea-denatured hemoprotein possessed increased nonenzymatic activity due to increased exposure of the protein-bound heme, however, peroxidase increased less than catalase which is consistent with the fact that peroxidase is the more heat stable enzyme. Nonenzymatic activity of the heat denatured hemoproteins was maximum when catalase was treated at 90 C for 2 min and peroxidase at 100 to 125 C for 5 to 30 min. © 1971 AOCS.
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| 4. |
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| 5. |
- Eriksson, Caj, et al.
(författare)
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Lipoxygenase from peas, purification and properties of the enzyme
- 1970
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Ingår i: BBA - Enzymology. - : Elsevier BV. - 0005-2744. ; 198:3, s. 449-459
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Tidskriftsartikel (refereegranskat)abstract
- 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.
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| 6. |
- Eriksson, Caj, et al.
(författare)
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Oxidation of fatty acids by heat treated hemoproteins
- 1970
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Ingår i: Lipids. - 0024-4201 .- 1558-9307. ; 5:3, s. 365-366
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Tidskriftsartikel (refereegranskat)abstract
- The hemoproteins catalase and peroxidase, after heat treatment which decreased their enzyme activities, became more efficient as heme catalysts of linoleic acid oxidation. These effects might be of importance for preservation and storage of food. © 1969 American Oil Chemists' Society.
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