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Functional activity of sporamin from sweet potato (Ipomoea batatas Lam.): a tuber storage protein with trypsin inhibitory activity
Abstract
Sporamin accounts for about 60% to 80% of total soluble protein in sweet potato tubers, and the predicted protein sequence of sporamin shares significant amino acid sequence identity with some Kunitz-type trypsin inhibitors. We constructed three recombinant plasmids with cDNAs that encode preprosporamin, prosporamin, and sporamin, and these three were expressed in Escherichia coli cells as fusion proteins. All three forms of sporamin expressed in E. coli were shown to have strong inhibitory activity to trypsin in vitro, suggesting that post-translational modifications are not essential for trypsin inhibitory activity. Northern blot analysis showed that sporamin transcripts could be systemically induced in leaf tissue of sweet potato by wounding. Therefore, sporamin may have a defense role as a protease inhibitor, in addition to its role as a storage protein.
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“Sporamins, which are the major storage proteins in sweet potato tuberous roots, belong to kunitz-type protease inhibitors and can be grouped into two subfamilies [49], [50], were abundant in some tissues, but very pool in other tissues.”
From Digital Gene Expression Analysis Based on Integrated De Novo Transcriptome Assembly of Sweet Potato [Ipomoea batatas (L.) Lam.] (2012) · cites this paper as [49]
In the citing paper
“Sporamins, which account for 60% to 80% of the total soluble proteins in sweet potato tuberous roots, belong to the PIs and are considered to be tuber-specific [49], [50].”
From Digital Gene Expression Analysis Based on Integrated De Novo Transcriptome Assembly of Sweet Potato [Ipomoea batatas (L.) Lam.] (2012) · cites this paper as [49]
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Metadata
- Authors
- Yeh, K.-W., Chen, J.-C., Lin, M.-I., Chen, Y.-M., & Lin, C.-Y.
- Affiliations
- National Taiwan University (TW)
- Venue
- Plant Molecular Biology
- Published
- 1997-02
- Volume
- 33
- Issue
- 3
- Pages
- 565-570
- ISSN
- 0167-4412 (ISSN-L)
- 1573-5028
- OpenAlex
- W2108960783
- Cited by
- 157
- References
- 31
- Citations by year
- 2026: 3 · 2025: 1 · 2024: 2 · 2023: 4 · 2022: 3 · 2021: 3 · 2020: 4 · 2019: 12 · 2018: 1 · 2017: 8 · 2016: 5 · 2015: 5 · 2014: 8 · 2012: 9
- FWCI
- 1.67
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- Locations
- Plant Molecular Biology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Science Council
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Protease and Inhibitor Mechanisms
- Life Sciences › Agricultural and Biological Sciences › Insect Science › Insect-Plant Interactions and Control
- Life Sciences › Agricultural and Biological Sciences › Plant Science › Plant Molecular Biology Research
- Keywords
- sporamin, Ipomoea batatas, trypsin inhibitor activity, Kunitz trypsin inhibitor, recombinant protein expression, post-translational modification, plant defense, protease inhibitors
- MeSH terms
- Amino Acid Sequence, Genetic Vectors, Molecular Sequence Data, Plant Proteins, Recombinant Fusion Proteins, Trypsin Inhibitor, Kunitz Soybean, Trypsin Inhibitors, Vegetables, Genes, Plant, Gene Expression Regulation, Plant, Plant Leaves, Plant Stems
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