A probarley lectin processing enzyme purified from Arabidopsis thaliana seeds

Asuman Mutlu, Joanne E. Pfeil, Susannah Gal

Research output: Contribution to journalArticle

28 Citations (Scopus)

Abstract

An aspartic proteinase was purified from the seeds of Arabidopsis thaliana (ecotype RLD) using affinity chromatography on pepstatin-agarose and ion exchange chromatography. The purified enzyme is optimally active at pH 3.5 and completely inhibited by pepstatin A. The purified Arabidopsis aspartic proteinase contains four subunits (apparent molecular weights 31, 28.5, 15 and 6 kDa), two of which are probably linked by disulfide bridges. These properties are similar to the aspartic proteinase previously isolated from barley seeds. The amino acid sequence of the peptide subunits corresponds exactly with the sequence of the previously isolated cDNA for the Arabidopsis aspartic proteinase. The Arabidopsis enzyme processed probarley lectin in vitro at the carboxy-terminus between phenylalanine and alanine, the same place where the barley enzyme cleaves the lectin in vitro. The aspartic proteinase appears to be the major enzyme processing the lectin in seeds as pepstatin A inhibited this activity in a crude seed extract.

Original languageEnglish (US)
Pages (from-to)1453-1459
Number of pages7
JournalPhytochemistry
Volume47
Issue number8
DOIs
StatePublished - Apr 1 1998

Fingerprint

Aspartic Acid Proteases
aspartic proteinases
Arabidopsis
Lectins
lectins
Seed
Seeds
Arabidopsis thaliana
Enzymes
Processing
enzymes
seeds
Hordeum
barley
Ecotype
Affinity chromatography
seed extracts
Ion Exchange Chromatography
ion exchange chromatography
affinity chromatography

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Plant Science
  • Horticulture

Cite this

Mutlu, Asuman ; Pfeil, Joanne E. ; Gal, Susannah. / A probarley lectin processing enzyme purified from Arabidopsis thaliana seeds. In: Phytochemistry. 1998 ; Vol. 47, No. 8. pp. 1453-1459.
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A probarley lectin processing enzyme purified from Arabidopsis thaliana seeds. / Mutlu, Asuman; Pfeil, Joanne E.; Gal, Susannah.

In: Phytochemistry, Vol. 47, No. 8, 01.04.1998, p. 1453-1459.

Research output: Contribution to journalArticle

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