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Dreesen TD, Dickens M, Koch RB. Partial purification and characterization of a Ca(2+)-stimulated lipoxygenase from soybean seeds. Lipids. 1982;17(12):964-9doi: 10.1007/BF02534593.
Dreesen, T. D., Dickens, M., & Koch, R. B. (1982). Partial purification and characterization of a Ca(2+)-stimulated lipoxygenase from soybean seeds. Lipids, 17(12), 964-9. https://doi.org/10.1007/BF02534593
Dreesen, T D, et al. "Partial purification and characterization of a Ca(2+)-stimulated lipoxygenase from soybean seeds." Lipids vol. 17,12 (1982): 964-9. doi: https://doi.org/10.1007/BF02534593
Dreesen TD, Dickens M, Koch RB. Partial purification and characterization of a Ca(2+)-stimulated lipoxygenase from soybean seeds. Lipids. 1982 Dec;17(12):964-9. doi: 10.1007/BF02534593. PMID: 27519438.
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Lipids. 1982 Dec;17(12):964-9. doi: 10.1007/BF02534593.

Partial purification and characterization of a Ca(2+)-stimulated lipoxygenase from soybean seeds.

Lipids

T D Dreesen, M Dickens, R B Koch

Affiliations

  1. Department of Biochemistry, Drawer BB, 39762, Mississippi State, MS.

PMID: 27519438 DOI: 10.1007/BF02534593

Abstract

A highly purified Ca(2+)-stimulated lipoxygenase was isolated from the Hill variety of soybean seeds. Separation of Ca(2+)-stimulated lipoxygenase from lipoxygenase active in the absence of Ca(2+) (lipoxygenase-1) was readily obtained using a DEAE-cellulose column. Sample size applied to the ion exchange column was found to be critical. Both enzymes were bound to the column, although some highly active Ca(2+)-stimulated lipoxygenase eluted with buffer in the presence of bound lipoxygenase-1. Ca(2+)-stimulated lipoxygenase bound to DAAE-cellulose required the use of a NaCl gradient for elution. Ca(2+)-stimulated lipoxygenase showed an apparent isoelectric point at pH 5.90 and optimum activity at pH 7.5 and at 1.1 mM calcium. Lipoxygenase-1 was inhibited over 95% in the presence of 60 μM methyl mercuric chloride, while Ca(2+)-stimulated lipoxygenase showed a maximum of only 20% inhibition under the same conditions.

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