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1998 | 20 | 2 |

Tytuł artykułu

Changes in the activity of phosphoenolpyruvate carboxylating enzymes in germinating yellow lupin seeds

Warianty tytułu

Języki publikacji

EN

Abstrakty

EN
The rate of phosphoenolpyruvate carboxylation by extracts from germinating lupin seeds was measured through the H¹⁴CO₃ fixation. PEP carboxylation in seed axes increased during their imbibition, mainly as a result of the increase in the activity of PEP carboxylase [EC 4.1.1.31]. However, the activity of PEP carboxykinase [EC 4.1.1.38], present during the first 3 hours of imbibition, as well as the activity of PEP-carboxykinase [EC 4.1.1.49], after 24 hours of imbibition, have also been shown. Possible physiological role of the changes in the activity of PEP carboxylases during lupin seeds germination is discussed.

Wydawca

-

Rocznik

Tom

20

Numer

2

Opis fizyczny

p.119-122

Twórcy

autor
  • A.Mickiewicz University, Al.Niepodleglosci 14, 61-713 Poznan, Poland
autor
autor
autor

Bibliografia

  • Andreo C. S., Gonzalez D., Iglesias A. 1987. Higher plant phosphoenolpyruvate carboxylase. Structure and regulation. FEBS Letters 213/1: 1–8
  • Bradford M.M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein, utilizing the principle of protein-dye binding. Anal. Biochem. 72:248–254.
  • Bryce J.H., Hill S.A. 1993. Energy production in plant cells. In: Plant Biochemistry and Molecular Biology, ed. by P.J. Lea, R.C. Leegood, John Wiley & Sons, Chichester 1–26.
  • Christeller J. T., Laing W.A., Suttow W.D. 1977. Carbon dioxide fixation by lupin root nodules. 1. Characterization, association with phosphoenolpyruvate carboxylase, and correlation with nitrogen fixation during nodule development. Plant Physiol. 60: 47–50.
  • Czosnowski E., Lorenc-Plucińska G., Jańczak-Dopierała B. 1978. Distribution and mobilization of reserve substances and localization of spherosomes in the cotyledons of Lupinus luteus L. cv.. Express. Bull. Soc. Amis. Sci. Poznań, serie D-18: 3–13.
  • Holdsworth E., Bruck K. 1977. Enzymes concerned with β-carboxylation in marine phytoplankter. Purification and properties of phosphoenolpyruvate carboxykinase. Arch. Biochem. Biophys. 182: 87–94.
  • Latzko E., Kelly G.J. 1983. The many faced function of phosphoenolpyruvate carboxylase in C3 plants. Physiol. Veg. 31: 805–815.
  • Leegood R.C. and Rees T. 1978. Phosphoenolpyruvate carboxykinase and gluconeogenesis in cotyledons of Cucurbita pepo. Biochim. Biophys. Acta 524: 207–218.
  • Lever M., Butler G.W. 1971. Precursors of asparagine in lupins. J. Exp. Bot. 22: 279–284.
  • Marczewski W. 1989. Phosphoenolpyruvate carboxylase in lupin nodules and roots. Identification of the enzymatic forms. Acta Biochim. Polonica 36: 31–36.
  • Perl M. 1978. Phosphoenol-pyruvate-carboxylase activity in cotton and sorghum seeds and its relation to seedling development. Planta 139: 239–243.
  • Perl M. 1986. ATP synthesis and utilization in the early stage of seeds germination in relation to seed dormancy and quality. Physiol. Plant. 66: 177–182.
  • Ratajczak W., Gierczak C., Ratajczak L. 1990. Changes in free amino acids levels at early stages of germination of yellow lupin seeds. Acta Physiol. Plant. 12: 253–258.
  • Ratajczak W., Lehmann T., Polcyn W., Ratajczak L. 1996. Metabolism of amino acids in germinating yellow lupin seeds. I. The decomposition of 14C-aspartate and 14C-glutamate during the imbibition. Acta Physiol. Plant. 18: 13–18.
  • Ratajczak W., Polcyn W., Lehmann T., Ratajczak L., Garnczarska M. 1998. Metabolism of amino acids in germinating lupin seeds. II. Pathway of conversion of aspartate to alanine during the imbibition. Acta Physiol. Plant. 20: 123–127.
  • Tomaszewska B., Mazurowa H., Schramm R.W. 1988. Activities of some enzymes of carbon metabolism connected with nitrogen fixation in the root nodules of the growing yellow lupin Lupinus luteus L. Acta Physiol. Plant. 10/2: 73–84.
  • Walker R., Trevanion S., Leegood R.C. 1995. Phosphoenolpyruvate carboxykinase from higher plants: purification from cucumber and evidence of rapid proteolytic cleavage in extracts from a range of plant tissues. Planta 196: 58–63.
  • Wojnowska T., Szymczyk S., Wojtas A., Sienkiewicz S. 1996. Skład chemiczny nasion trzech odmian łubinu żółtego. (Chemical composition of three varieties of yellow lupin). Łubin: kierunki badań i perspektywy użytkowe wyd., Polskie Towarzystwo Łubinowe., Poznań: 177–185.

Typ dokumentu

Bibliografia

Identyfikatory

Identyfikator YADDA

bwmeta1.element.agro-article-024fd2d9-035e-4ea1-a733-7490468ca216
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