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. 1989 Mar;89(3):952–957. doi: 10.1104/pp.89.3.952

Regulation of Catalase Activity in Leaves of Nicotiana sylvestris by High CO2

Evelyn A Havir 1, Neil A McHale 1
PMCID: PMC1055949  PMID: 16666647

Abstract

The effect of high CO2 (1% CO2/21% O2) on the activity of specific forms of catalase (CAT-1, -2, and -3) (EA Havir, NA McHale [1987] Plant Physiol 84: 450-455) in seedling leaves of tobacco (Nicotiana sylvestris, Nicotlana tabacum) was examined. In high CO2, total catalase activity decreased by 50% in the first 2 days, followed by a more gradual decline in the next 4 days. The loss of total activity resulted primarily from a decrease in CAT-1 catalase. In contrast, the activity of CAT-3 catalase, a form with enhanced peroxidatic activity, increased 3-fold in high CO2 relative to air controls after 4 days. Short-term exposure to high CO2 indicated that the 50% loss of total activity occurs in the first 12 hours. Catalase levels increased to normal within 12 hours after seedlings were returned to air. When seedlings were transferred to air after prolonged exposure to high CO2 (13 days), the levels of CAT-1 catalase were partially restored while CAT-3 remained at its elevated level. Levels of superoxide dismutase activity and those of several peroxisomal enzymes were not affected by high CO2. Total catalase levels did not decline when seedlings were exposed to atmospheres of 0.04% CO2/5% O2 or 0.04% CO2/1% O2, indicating that regulation of catalase in high CO2 is not related directly to suppression of photorespiration. Antibodies prepared against CAT-1 catalase from N. tabacum reacted strongly against CAT-1 catalase from both N. sylvestris and N. tabacum but not against CAT-3 catalase from either species. This observation, along with the rapid changes in CAT-1 and the much slower changes in CAT-3 suggest that one form is not directly derived from the other.

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Selected References

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  1. Bradford M. M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem. 1976 May 7;72:248–254. doi: 10.1006/abio.1976.9999. [DOI] [PubMed] [Google Scholar]
  2. Clare D. A., Duong M. N., Darr D., Archibald F., Fridovich I. Effects of molecular oxygen on detection of superoxide radical with nitroblue tetrazolium and on activity stains for catalase. Anal Biochem. 1984 Aug 1;140(2):532–537. doi: 10.1016/0003-2697(84)90204-5. [DOI] [PubMed] [Google Scholar]
  3. Eising R., Gerhardt B. Catalase Degradation in Sunflower Cotyledons during Peroxisome Transition from Glyoxysomal to Leaf Peroxisomal Function. Plant Physiol. 1987 Jun;84(2):225–232. doi: 10.1104/pp.84.2.225. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Feierabend J., Beevers H. Developmental studies on microbodies in wheat leaves : I. Conditions influencing enzyme development. Plant Physiol. 1972 Jan;49(1):28–32. doi: 10.1104/pp.49.1.28. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Flohé L., Otting F. Superoxide dismutase assays. Methods Enzymol. 1984;105:93–104. doi: 10.1016/s0076-6879(84)05013-8. [DOI] [PubMed] [Google Scholar]
  6. Gershoni J. M., Palade G. E. Protein blotting: principles and applications. Anal Biochem. 1983 May;131(1):1–15. doi: 10.1016/0003-2697(83)90128-8. [DOI] [PubMed] [Google Scholar]
  7. Havir E. A. Evidence for the presence in tobacco leaves of multiple enzymes for the oxidation of glycolate and glyoxylate. Plant Physiol. 1983 Apr;71(4):874–878. doi: 10.1104/pp.71.4.874. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Havir E. A., McHale N. A. Biochemical and developmental characterization of multiple forms of catalase in tobacco leaves. Plant Physiol. 1987 Jun;84(2):450–455. doi: 10.1104/pp.84.2.450. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Havir E. A. Phenylalanine ammonia-lyase: purification and characterization from soybean cell suspension cultures. Arch Biochem Biophys. 1981 Oct 15;211(2):556–563. doi: 10.1016/0003-9861(81)90490-2. [DOI] [PubMed] [Google Scholar]
  10. Hendricks S. B., Taylorson R. B. Breaking of seed dormancy by catalase inhibition. Proc Natl Acad Sci U S A. 1975 Jan;72(1):306–309. doi: 10.1073/pnas.72.1.306. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Kunce C. M., Trelease R. N. Heterogeneity of catalase in maturing and germinated cotton seeds. Plant Physiol. 1986 Aug;81(4):1134–1139. doi: 10.1104/pp.81.4.1134. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Kunce C. M., Trelease R. N., Turley R. B. Purification and biosynthesis of cottonseed (Gossypium hirsutum L.) catalase. Biochem J. 1988 Apr 1;251(1):147–155. doi: 10.1042/bj2510147. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
  14. Nir G., Shulman Y., Fanberstein L., Lavee S. Changes in the Activity of Catalase (EC 1.11.1.6) in Relation to the Dormancy of Grapevine (Vitis vinifera L.) Buds. Plant Physiol. 1986 Aug;81(4):1140–1142. doi: 10.1104/pp.81.4.1140. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Omran R. G. Peroxide Levels and the Activities of Catalase, Peroxidase, and Indoleacetic Acid Oxidase during and after Chilling Cucumber Seedlings. Plant Physiol. 1980 Feb;65(2):407–408. doi: 10.1104/pp.65.2.407. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Rich P. R., Boveris A., Bonner W. D., Jr, Moore A. L. Hydrogen peroxide generation by the alternate oxidase of higher plants. Biochem Biophys Res Commun. 1976 Aug 9;71(3):695–703. doi: 10.1016/0006-291x(76)90887-1. [DOI] [PubMed] [Google Scholar]
  17. Srivastava S. K., Ansari N. H. The peroxidatic and catalatic activity of catalase in normal and acatalasemic mouse liver. Biochim Biophys Acta. 1980 Dec 15;633(3):317–322. doi: 10.1016/0304-4165(80)90191-9. [DOI] [PubMed] [Google Scholar]
  18. Tsaftaris A. S., Bosabalidis A. M., Scandalios J. G. Cell-type-specific gene expression and acatalasemic peroxisomes in a null Cat2 catalase mutant of maize. Proc Natl Acad Sci U S A. 1983 Jul;80(14):4455–4459. doi: 10.1073/pnas.80.14.4455. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Yamaguchi J., Nishimura M., Akazawa T. Maturation of catalase precursor proceeds to a different extent in glyoxysomes and leaf peroxisomes of pumpkin cotyledons. Proc Natl Acad Sci U S A. 1984 Aug;81(15):4809–4813. doi: 10.1073/pnas.81.15.4809. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. ZELITCH I., OCHOA S. Oxidation and reduction of glycolic and glyoxylic acids in plants. I. Glycolic and oxidase. J Biol Chem. 1953 Apr;201(2):707–718. [PubMed] [Google Scholar]

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