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Isolation and characterization of 5-lipoxygenase from tulip bulbs

โœ Scribed by P. Reddanna; J. Whelan; P.S. Reddy; C.C. Reddy


Book ID
117058469
Publisher
Elsevier Science
Year
1988
Tongue
English
Weight
317 KB
Volume
157
Category
Article
ISSN
0006-291X

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โœฆ Synopsis


An unique membrane bound lipoxygenase was isolated and purified from purple star tulip bulbs with a specific activity of 5.2 mu moles O2 consumed.min-1.mg-1 protein. The purified tulip enzyme exhibits regiospecificity for O2 insertion at C-5 of the arachidonic acid molecule. Identification of the reaction product was confirmed as 5-hydroperoxyeicosatetraenoic acid by analytical criteria which included: cochromatography with the authentic compound, as well as mass spectral and 1H-NMR analysis. Thus, the enzyme from tulip bulbs appears to be different from the cytosolic lipoxygenase from potato tubers, which exhibits non-regiospecificity in terms of O2 incorporation. However, the purified tulip lipoxygenase showed a strong immunological crossreactivity with antiserum raised against the purified potato lipoxygenase, indicating close immunological relationship with the other plant lipoxygenases.


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