Complete amino acid sequence of chitinase-a from bulbs of gladiolus (gladiolus gandavensis)

Takeshi Yamagami, Yoichiro Mine, Masatsune Ishiguro

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14 Citations (Scopus)

Abstract

The complete amino acid sequence of gladiolus bulb chitinase-a (GBC-a) was determined. First the tryptic peptides from GBC-a after it was reduced and S-carboxymethylated were sequenced and then the peptides were further studied by chemical cleavage of the enzyme. GBC-a consisted of 274 amino acid residues and had a molecular mass of 30,714 Da. Two consensus sequences essential forchitinase activity by plant class III chitinases were conserved in GBC-a, although its sequence similarity with plant class III chitinases was less than 20%. Sequence comparison of GBC-a with sequences of other proteins in a protein identification resource (PIR) showed that the GBC-a sequence was 33% similar to that of narbonin, a seed storage 2S globulin from narbon be.

Original languageEnglish
Pages (from-to)386-389
Number of pages4
JournalBioscience, Biotechnology and Biochemistry
Volume62
Issue number2
DOIs
Publication statusPublished - 1998

All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Analytical Chemistry
  • Biochemistry
  • Applied Microbiology and Biotechnology
  • Molecular Biology
  • Organic Chemistry

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