Purification and partial characterization of three genetically defined catalases of maize

Chandlee, Joel M.; Tsaftaris, Athanasios; Scandalios, John G.

doi:10.1016/0304-4211(83)90136-0

Cited by 69 publications

(59 citation statements)

References 18 publications

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“…In this tissue, the isozyme was abundant early in development (about 12 cm2/mg protein at d 4 PI) and subsequently decreased by about 40% at d 12 PI. The level of CAT-3 in the d 4 PI shoots of greenhouse grown plants was about the same as that in the epicotyl (Fig. 2B, open circles).…”

Section: Resultsmentioning

confidence: 57%

“…The Fig. 4 The maize primary root breaks through the pericarp early in germination (12) and, for this study, was first isolated on d 4 PI. By d 6 PI, lateral seminal roots had formed, with adventitious roots becoming dominant by d 14 PI.…”

Section: Resultsmentioning

confidence: 99%

“…(15), using BSA (Sigma, fraction V) as a standard. The levels ofCAT-2 and CAT-3 protein were determined by rocket immunoelectrophoresis using isozyme-specific anti-CAT-2 and anti-CAT-3 sera as described (4 (2). The sense RNA used as standards was transcribed using plasmids digested with the appropriate endonuclease immediately 3' to the insert DNA.…”

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confidence: 99%

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The Distribution of Catalase Activity, Isozyme Protein, and Transcript in the Tissues of the Developing Maize Seedling

Redinbaugh¹,

Sabre²,

Scandalios³

1990

Plant Physiol.

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The catalase activity, CAT-2 and CAT-3 isozyme protein levels, and the steady-state mRNA levels for each of the three catalase genes were determined in the scutellum, root, epicotyl, and leaf of the developing maize (Zea mays L.) seedling. Catalase activity was highest in the scutellum, with 10-fold lower enzyme activity in the leaf and epicotyl. Very low levels of catalase activity were found in the root. The highest levels of CAT-2 protein were found in the scutellum, with about 10-fold lower levels in the green leaf.

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Section: Resultsmentioning

confidence: 57%

Section: Resultsmentioning

confidence: 99%

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The Distribution of Catalase Activity, Isozyme Protein, and Transcript in the Tissues of the Developing Maize Seedling

Redinbaugh¹,

Sabre²,

Scandalios³

1990

Plant Physiol.

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“…For example, EP-CAT from tobacco and maize is more sensitive to temperature than is T-CAT (1,4). The expression of T-CAT from both maize and barley is light dependent but that of EP-CAT is not (18; this paper), and maize EP-CAT has been shown to be less sensitive to the inhibitor 3-amino -I,2,4-triazole than T-CAT (1).…”

Section: Discussionmentioning

confidence: 93%

Enhanced-Peroxidatic Activity in Specific Catalase Isozymes of Tobacco, Barley, and Maize

Havir

McHale²

1989

Plant Physiol.

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Separation of catalase isozymes from leaf extracts of three diverse plant species (Nicotiana sylvestris, Zea mays, Hordeum vulgare L.) revealed a distinct isozyme with enhanced peroxidatic activity (30-, 70-, 28-fold over typical catalase, respectively) which constituted 10 to 20% of the total catalase activity. In maize this isozyme is the product of the Cat3 gene, which is expressed only in mesophyll cells (AS Tsaftaris, AM Bosabalidis, JG Scandalios [1983] Proc NatI Acad Sci USA 80: 4455-4459). A mutation in barley reducing levels of peroxisomal catalase (AC Kendall et al. [1983] Planta 159: 505-511) does not reduce the amount of the isozyme with enhanced peroxidatic activity. Similarly, this isozyme is unaffected in dark-grown barley in spite of a 75% decrease in total catalase activity. These results suggest that this catalase isozyme is under separate genetic control in barley. This may also be the case in tobacco where the catalase isozyme with enhanced peroxidatic activity is an immunologically distinct protein (EA Havir, NA McHale [1989] Plant Physiol 89: 952-957).

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“…AT inhibits CAT1 by 93%, CAT2 by 98%, and CAT3 by 32% (Chandlee et al, 1983) allowing differences in CAT3 activity among treatments to be monitored with little interference from other isozymes. All acclimation and ABA treatments were replicated three times and activity was analyzed as a factorial design with acclimation or ABA treatment, chilling, and replication as the factors.…”

Section: Catalase Activitymentioning

confidence: 99%

Molecular and biochemical investigation of the mechanisms of acclimation to chilling stress in maize seedlings

Anderson

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Purification and partial characterization of three genetically defined catalases of maize

Cited by 69 publications

References 18 publications

The Distribution of Catalase Activity, Isozyme Protein, and Transcript in the Tissues of the Developing Maize Seedling

The Distribution of Catalase Activity, Isozyme Protein, and Transcript in the Tissues of the Developing Maize Seedling

Enhanced-Peroxidatic Activity in Specific Catalase Isozymes of Tobacco, Barley, and Maize

Molecular and biochemical investigation of the mechanisms of acclimation to chilling stress in maize seedlings

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