Immunological comparison of lipoxygenase isozymes-1 and -2 with soybean seedling lipoxygenases

Tk, Peterman; Jn, Siedow

doi:10.1016/0003-9861(85)90190-0

Cited by 22 publications

(11 citation statements)

References 12 publications

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“…The soybean LOX L-1-specific antibodies cross-reacted with soybean LOX L-l, L-2, and L-3 protein preparations, with a stronger reaction to soybean LOX L-l (Fig. 3), a result similar to that reported earlier (Peterman and Siedow, 1985). The tomato 94-kD-specific antibodies cross-reacted with all three soybean isozyme preparations, but a stronger reaction was obtained with the soybean LOX L-2 preparation than with the soybean LOX L-l and L-3 preparations (Fig.…”

Section: The 94-kd Protein Is a Member Of The Lipoxygenase Gene Familysupporting

confidence: 88%

Molecular Cloning of a Ripening-Specific Lipoxygenase and Its Expression during Wild-Type and Mutant Tomato Fruit Development

Kausch

Handa

1997

Plant Physiology

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A 94-kD protein that accumulates predominately in tomato (Lycopersicon esculenfum) fruit during ripening was purified, and antibodies specific for the purified protein were used to isolate cDNA clones from a red-ripe fruit cDNA library. A sequence analysis of these cDNAs and cross-reactivity of the 94-kD-specific antibodies to the soybean lipoxygenase (LOX) L-1, L-2, and L-3 proteins and soybean LOX L-l-specific antibodies to the 94-kD protein identified it as a member of the LOX gene family. Maximum levels of the 94-kD LOX mRNA and protein are present in breaker to ripe and red-ripe stages, respectively. Expression of 94-kD LOX in different tissues from mature green and red-ripe tomato fruits was found to be greatest in the radial walls of ripe fruit, but immunocytolocalization using tissue printing suggests that the highest accumulation of its protein occurs in locular jelly. None of 94-kD LOX is expressed in nonripening mutant fruits of any age. Never-ripe mutant fruit accumulate the 94-kD LOX mRNA to levels similar to those obtained in wild-type fruit, but fail to accumulate the 94-kD LOX protein. Collectively, the results show that expression of 94-kD LOX is regulated by the ripening process, and ethylene may play a role in its protein accumulation.

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Section: The 94-kd Protein Is a Member Of The Lipoxygenase Gene Familysupporting

confidence: 88%

Molecular Cloning of a Ripening-Specific Lipoxygenase and Its Expression during Wild-Type and Mutant Tomato Fruit Development

Kausch

Handa

1997

Plant Physiology

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“…After two brief rinses in TEST, the filters were incubated in TEST for 15 min, followed by two additional washes of 5 min each. The filters were then incubated for 2 h with rabbit antisoybean lipoxygenase-2 antibodies (Peterman and Siedow, 1985a) diluted 1:2000 in quench solution. Following incubation with primary antibodies, the filters were rinsed twice with TEST and washed once for 15 min and twice for 5 min each in TEST.…”

Section: Iefmentioning

confidence: 99%

The Lipoxygenase Isozymes in Soybean [Glycine max (L.) Merr.] Leaves (Changes during Leaf Development, after Wounding, and following Reproductive Sink Removal)

Saravitz

Siedow

1995

Plant Physiol.

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The levels of individual lipoxygenase isozymes in soybean [Clycine max (1.) Merr.] leaves were assessed during leaf development, after mechanical wounding, and i n response to reproductive sink removal. Native isoelectric focusing followed by immunoblotting was employed to examine individual lipoxygenase isozymes. In leaves of all ages, two distinct classes of lipoxygenase isozymes were detected. One class of lipoxygenase isozymes had nearly neutral isoelectric points (pls) ranging from pH 6.8 to 7.2. The other class of lipoxygenase isozymes had acidic pls ranging from pH 4.7 to 5.6. During leaf development, all of the neutral lipoxygenase isozymes and most of the acidic isozymes were present in greatest abundance in the youngest leaves examined and declined in amount as leaf age increased. However, four acidic lipoxygenase isozymes (pl = 4.70, 4.80, 4.90, 4.95) were more abundant in intermediateage leaves than in either the youngest or oldest leaves examined.Following mechanical wounding of leaves, these same four acidic isozymes also increased i n abundance both locally and systemically in leaves from wounded plants. Unlike the specific effects of wounding on the lipoxygenase isozymes in leaves, reproductive sink removal stimulated a general increase in most of the acidic lipoxygenase isozymes in leaves.

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“…Such (23). An affinity-purified antilipoxygenase-2 was developed in rabbits immunized with purified, native soybean lipoxygenase-2, and it has been shown to cross-react with soybean seed lipoxygenases-1, -2, and -3 on immunoblots (21).…”

mentioning

confidence: 99%

Behavior of Lipoxygenase during Establishment, Senescence, and Rejuvenation of Soybean Cotyledons

Peterman¹,

Siedow²

1985

Plant Physiol.

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ABSTRACILipoxygenase protein and activity were examined during establishment, senescence, and rejuvenation of soybean cotyledons. Lipoxygenase protein, as determined on 'Western' immunoblots, and lipoxygenase-l and -2/3 activities decreased during mobilization of seed reserves 3 to 9 days following planting. Lipoxygenase-l activity decreased more rapidly than lipoxygenase-2/3 and was not detectable by 11 days after planting. Lipoxygenase protein increased after day 11 while lipoxygenase-2/3 activity continued to decline. During the later stages of cotyledon senescence, both lipoxygenase protein and lipoxygenase-2/3 activity decreased. Upon rejuvenation, lipoxygenase-2/3 activity, but not that of lipoxygenase-l, increased. These results demonstrate that elevated lipoxygenase activity does not represent a universal characteristic of senescent plant tissue.The senescence of cotyledons on dicotyledonous plants, like leaf senescence, represents a genetically programmed sequence of events which ultimately results in the deterioration of mature cells (27). Senescing cotyledons undergo a number of complex ultrastructural and metabolic changes. Protein, DNA, RNA, and Chl levels progressively decline (4,11,27). A large number of enzyme activities change during senescence (4, 16). Senescence of soybean cotyledons is also accompanied by a decrease in translational capacity as measured in vitro by the ability of isolated ribosomes and supernatant fractions to carry out the polyuridylic acid-directed incorporation of phenylalanine (22) and in vivo by 35S-methionine incorporation into protein by cotyledon discs (24). This decrease in total translational capacity does not represent a specific decrease in the synthesis of all proteins (24) and has been associated with a decrease in both mRNA (3, 24) and polysomes (3).A decrease in membrane integrity and loss of cellular compartmentation are also observed during cotyledon senescence. Electron micrographs of soybean cotyledons (28) reveal the disruption and loss of both organelle and plasma membranes during the later stages of senescence. As senescence progresses in Phaseolus vulgaris cotyledons, the lipid phase transition temperature, measured by x-ray diffraction, increases and an increased proportion of isolated microsomal membranes exists in a gelphase at physiological temperatures (17). The resulting combination of gel and liquid-crystalline phases within the bilayer

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Immunological comparison of lipoxygenase isozymes-1 and -2 with soybean seedling lipoxygenases

Cited by 22 publications

References 12 publications

Molecular Cloning of a Ripening-Specific Lipoxygenase and Its Expression during Wild-Type and Mutant Tomato Fruit Development

Molecular Cloning of a Ripening-Specific Lipoxygenase and Its Expression during Wild-Type and Mutant Tomato Fruit Development

The Lipoxygenase Isozymes in Soybean [Glycine max (L.) Merr.] Leaves (Changes during Leaf Development, after Wounding, and following Reproductive Sink Removal)

Behavior of Lipoxygenase during Establishment, Senescence, and Rejuvenation of Soybean Cotyledons

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