PMID: 9532802Apr 9, 1998Paper

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

Bioscience, Biotechnology, and Biochemistry
T YamagamiM Ishiguro

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 for chitinase 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 beans.

References

Jan 1, 1993·The Plant Journal : for Cell and Molecular Biology·D B CollingeK Vad
Mar 1, 1995·Acta Crystallographica. Section D, Biological Crystallography·M HennigV H Nong

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