Journal article
Isolation and characterisation of full-length cDNA clones of the giant taro (Alocasia macrorrhiza) trypsin/chymotrypsin inhibitor
Plant Molecular Biology Reporter, Vol.30(5), pp.1035-1039
1996
Abstract
A full-length cDNA encoding the 206 amino acid open reading frame of a trypsin/chymotrypsin inhibitor abundant in the corms of giant taro (Alocasia macrorrhiza) was isolated. An internal fragment was cloned using degenerate primers corresponding to a region of the mature protein sequence and the ‘rapid amplification of cDNA ends’ (RACE) method used to generate a composite cDNA sequence. The length of the cDNA was close to the predicted size of the corresponding transcript deduced from northern blot analysis of corm mRNA. The inhibitor was expressed strongly in the mature corm, at low levels in leaf blades and petioles but not in roots. Southern blot analysis of the giant taro DNA indicated that this inhibitor is encoded by a small multigene family and this was further supported by the isolation of two different sequence classes from corm cDNA using primers to the ends of the composite sequence.
Details
- Title
- Isolation and characterisation of full-length cDNA clones of the giant taro (Alocasia macrorrhiza) trypsin/chymotrypsin inhibitor
- Authors/Creators
- A. Mathews (Author/Creator)D.J. Llewellyn (Author/Creator)Y. Wu (Author/Creator)E.S. Dennis (Author/Creator)
- Publication Details
- Plant Molecular Biology Reporter, Vol.30(5), pp.1035-1039
- Publisher
- Springer New York
- Identifiers
- 991005544152307891
- Murdoch Affiliation
- State Agricultural Biotechnology Centre
- Language
- English
- Resource Type
- Journal article
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- Citation topics
- 3 Agriculture, Environment & Ecology
- 3.180 Microbial Biotechnology
- 3.180.867 Protease Inhibitors
- Web Of Science research areas
- Biochemistry & Molecular Biology
- Plant Sciences
- ESI research areas
- Plant & Animal Science