Abstract:
:Membrane-associated lipoxygenase from green tomato (Lycopersicon esculentum L. cv Caruso) fruit has been purified 49-fold to a specific activity of 8.3 mumol.min(-1).mg(-1) of protein by solubilization of microsomal membranes with Triton X-100, followed by anion- exchange and size-exclusion chromatography. The apparent molecular mass of the enzyme was estimated to be 97 and 102 kD by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and size-exclusion chromatography, respectively. The purified membrane lipoxygenase preparation consisted of a single major band following sodium dodecyl sulfate-polyacrylamide gel electrophoresis, which cross-reacts with immunoserum raised against soluble soybean lipoxygenase 1. It has a pH optimum of 6.5, an apparent K(m) of 6.2 mum, and V(max) of 103. mumol.min(-1).mg(-1) of protein with linoleic acid as substrate. Corresponding values for the partially purified soluble lipoxygenase from tomato are 3.8 mum and 1.3 mumol.min(-1).mg(-1) of protein, respectively. Thus, the membrane-associated enzyme is kinetically distinguishable from its soluble counterpart. Sucrose density gradient fractionation of the isolated membranes indicated that the membrane-associated lipoxygenase sediments with thylakoids. A lipoxygenase band with a corresponding apparent mol wt of 97,000 was identified immunologically in sodium dodecyl sulfate-polyacrylamide gel electrophoresis-resolved proteins of purified thylakoids prepared from intact chloroplasts isolated from tomato leaves and fruit.
journal_name
Plant Physioljournal_title
Plant physiologyauthors
Bowsher CG,Ferrie BJ,Ghosh S,Todd J,Thompson JE,Rothstein SJdoi
10.1104/pp.100.4.1802subject
Has Abstractpub_date
1992-12-01 00:00:00pages
1802-7issue
4eissn
0032-0889issn
1532-2548journal_volume
100pub_type
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