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2005 | 27 | 4A |

Tytuł artykułu

Carboxypeptidases of germinating triticale grains

Warianty tytułu

Języki publikacji

EN

Abstrakty

EN
Presence of five carboxypeptidases was found in endosperm of germinating triticale grains, while two of them in scutellum. Changes of their activities during four days of germination suggest that carboxypeptidase II plays an important role at initial stage of germination, while carboxypeptidases I and III - at subsequent stages of the process. High activity of carboxyt peptidase II both in scutellum and endosperm of dry grains accompanied by its decrease during germination, and on the other hand, the appearance of carboxypeptidases I and III activities at the 2nd and 3rd day of the process seems to confirm such functions of these enzymes. Experiments with GA3 indicated that carboxypeptidase I was synthesized in scutellum, and carboxypeptidase III - in aleurone layer. Carboxypeptidases I and II cleave N-CBZ-Phe-Ala, and carboxypeptidase III - N-CBZ-Ala-Met and N-CBZ-Ala-Phe as substrates with the highest rate.

Wydawca

-

Rocznik

Tom

27

Numer

4A

Opis fizyczny

p.539-547,fig.,ref.

Twórcy

autor
  • Warsaw Agricultural University, Nowoursynowska 159, 02-776 Warsaw, Poland
autor
autor

Bibliografia

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  • Breddam K., Sorensen S.B., Ottesen M. 1985. Isolation of carboxypeptidase II from malted barley by affinity chromatography. Carlsberg Res. Commun. 50: 199209.
  • Breddam K. 1986. Serine carboxypeptidases. A review. Carlsberg Res. Commun. 51: 83-128.
  • Breddam K., Sorensen S.B. 1987. Isotation of carbs oxypeptidase III from malted barley by affinity chromatography. Carlsberg Res. Commun. 52: 275-283.
  • Breddam K., Sorensen S.B., Svendsen I. 1987. Pris mary structure and enzymatic properties of carboxypeptidase II from wheat bran. Carlsberg Res. Commun. 52: 297-311.
  • Dal Degan F., Rocher A., Cameron-Mills V., von Wettstein D. 1994. The expression of serine carboxy- peptidases during maturation and germination of the barley grain. Proc. Natl. Acad. Sci. USA 91: 8209-8213.
  • Davy A., Svendsen I., Sorensen S.O., Sorensen M.B., Rouster J., Meldal M., Simpson D.J., Cameron-Mills V. 1998. Substrate specificity of barley cysteine endo-peptidases EP-A and EP-B. Plant Physiol. 117: 255-261.
  • Dominguez F., Cejudo F.J. 1998. Germination-related genes encoding proteolytic enzymes are expressed in the nucellus of developing wheat grains. Plant J. 15: 569-574
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  • Jivotovskaya A.V., Horstmann C., Vaintraub I.A. 1997. Desecsion of the isoenzymes of wheat grain proteinase A. Phytochemistry 45: 1549-1553.
  • Mikola J., Kolehmainen L. 1972. Localization and activity of various peptidases in germinating barley. Planta 104: 167-177.
  • Mikola L. 1983. Germinating barley grains contain five acid carboxypeptidases with complementary substrate specificities. Biochim. Biophys. Acta 747: 241-252.
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  • Okamoto T., Yuki A., Mitsuhashi N., Mimamikawa T. 1999. Asparaginyl endopeptidase (VmPE-1) and autocatalytic processing synergistically activate the vacuolar cysteine proteinase (SH-EP). Eur. J. Biochem. 264: 223-232.
  • Potokina E., Sreenivasulu N., Altschmied L., Michalek W., Graner A. 2002. Differential gene expression during seed germination in barley (Hordeum vulgare L.). Funct. Integr. Genomics 2: 28-39.
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  • Runeberg-Roos P., Tormakangas K., Ostman A. 1991. Primary structure of a barley-grain proteinase (A plant aspartic proteinase resembling mammalian cathepsin D). Eur. J. Biochem. 202: 1021-1027.
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Typ dokumentu

Bibliografia

Identyfikatory

Identyfikator YADDA

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