Literature DB >> 16668566

Turnover of catalase heme and apoprotein moieties in cotyledons of sunflower seedlings.

R Eising1, B Süselbeck.   

Abstract

The turnover of catalase apoprotein and catalase heme was studied in cotyledons of sunflower (Helianthus annuus L.) seedlings by density labeling of apoprotein and radioactive labeling of heme moieties. The heavy isotope (50% (2)H(2)O) and the radioactive isotope ([(14)C]5-aminolevulinic acid) were applied either during growth in the dark (day 0-2.5) or in the light (day 2.5 and 5). Following isopycnic centrifugation of catalase purified from cotyledons of 5-day-old seedlings, superimposition curve fitting was used to determine the amounts of radioactive heme moieties in native and density-labeled catalase. Data from these determinations indicated that turnover of catalase heme and apoprotein essentially was coordinate. Only small amounts of heme groups were recycled into newly synthesized apoprotein during growth in the light, and no evidence was found for an exchange of heme groups in apoprotein moieties. It followed from these observations that degradation of catalase apoprotein was slightly faster than that of catalase heme. A degradation constant for catalase apoprotein of 0.263 per day was determined from the data on heme recycling and the degradation constant of catalase heme determined previously to be 0.205 per day (R Eising, B Gerhardt [1987] Plant Physiol 84: 225-232).

Entities:  

Year:  1991        PMID: 16668566      PMCID: PMC1081181          DOI: 10.1104/pp.97.4.1422

Source DB:  PubMed          Journal:  Plant Physiol        ISSN: 0032-0889            Impact factor:   8.340


  17 in total

1.  Transition form of microbodies. Overlapping of two sets of marker proteins during the rearrangement of glyoxysomes into leaf peroxisomes.

Authors:  W Behrends; R Birkhan; H Kindl
Journal:  Biol Chem Hoppe Seyler       Date:  1990-01

2.  The kinetics of disappearance of labeled leucine from the free leucine pool of rat liver and its effect on the apparent turnover of catalase and other hepatic proteins.

Authors:  B Poole
Journal:  J Biol Chem       Date:  1971-11       Impact factor: 5.157

3.  Turnover of heme and protein moieties of rat liver microsomal cytochrome b5.

Authors:  K W Bock; P Siekevitz
Journal:  Biochem Biophys Res Commun       Date:  1970-10-23       Impact factor: 3.575

Review 4.  Biogenesis of peroxisomes.

Authors:  P B Lazarow; Y Fujiki
Journal:  Annu Rev Cell Biol       Date:  1985

5.  Immature precursor catalase in subcellular fractions of rat liver.

Authors:  Y Sugita; T Tobe; T Sakamoto; T Higashi
Journal:  J Biochem       Date:  1982-08       Impact factor: 3.387

6.  The in vivo turnover of rat liver microsomal epoxide hydrolase and both the apoprotein and heme moieties of specific cytochrome P-450 isozymes.

Authors:  A Parkinson; P E Thomas; D E Ryan; W Levin
Journal:  Arch Biochem Biophys       Date:  1983-08       Impact factor: 4.013

7.  Enzymic capacities for chlorophyll biosynthesis. Activation and de novo synthesis of enzymes.

Authors:  H A Schneider
Journal:  Z Naturforsch C Biosci       Date:  1976 Jan-Feb

8.  The synthesis and turnover of rat liver peroxisomes. V. Intracellular pathway of catalase synthesis.

Authors:  P B Lazarow; C de Duve
Journal:  J Cell Biol       Date:  1973-11       Impact factor: 10.539

9.  The synthesis and turnover of rat liver of rat liver peroxisomes. IV. Biochemical pathway of catalase synthesis.

Authors:  P B Lazarow; C de Duve
Journal:  J Cell Biol       Date:  1973-11       Impact factor: 10.539

10.  The synthesis and turnover of rat liver peroxisomes. II. Turnover of peroxisome proteins.

Authors:  B Poole; F Leighton; C De Duve
Journal:  J Cell Biol       Date:  1969-05       Impact factor: 10.539

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  3 in total

1.  Novel insights in mammalian catalase heme maturation: effect of NO and thioredoxin-1.

Authors:  Ritu Chakravarti; Karishma Gupta; Alana Majors; Lisa Ruple; Mark Aronica; Dennis J Stuehr
Journal:  Free Radic Biol Med       Date:  2015-02-04       Impact factor: 7.376

2.  Immunogold labelling indicates high catalase concentrations in amorphous and crystalline inclusions of sunflower (Helianthus annuus L.) peroxisomes.

Authors:  K B Tenberge; R Eising
Journal:  Histochem J       Date:  1995-03

3.  Vitiligo: a possible model of degenerative diseases.

Authors:  Barbara Bellei; Angela Pitisci; Monica Ottaviani; Matteo Ludovici; Carlo Cota; Fabiola Luzi; Maria Lucia Dell'Anna; Mauro Picardo
Journal:  PLoS One       Date:  2013-03-26       Impact factor: 3.240

  3 in total

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