The DOI matches its Crossref record; 31 of the 31 references it cites were found in a registry or an index.
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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In the citing paper
“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]
Citations
Cites
Molecular Cloning: A Laboratory Manual
Sambrook, J., Fritsch, E., & Maniatis, T. (1989) · UCLA - Biblioteca de Ciencias de la Salud · Cited by 133,589
A comprehensive set of sequence analysis programs for the VAX
Devereux, J., Haeberli, P. E., & Smithies, O. (1984) · Nucleic Acids Research · doi:10.1093/nar/12.1part1.387 · Cited by 14,222
Smith, D. B., & Johnson, K. S. (1988) · Gene · doi:10.1016/0378-1119(88)90005-4 · Cited by 5,844
Wound-Induced Proteinase Inhibitor in Plant Leaves: A Possible Defense Mechanism against Insects
Green, T. R., & Ryan, C. A. (1972) · Science · doi:10.1126/science.175.4023.776 · Cited by 1,179
DEFENSE-RELATED PROTEINS IN HIGHER PLANTS
Bowles, D. J. (1990) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.59.070190.004301 · Cited by 1,043
A novel mechanism of insect resistance engineered into tobacco
Hilder, V. A., Gatehouse, A. M. R., Sheerman, S. E., Barker, R. F., & Boulter, D. (1987) · Nature · doi:10.1038/330160a0 · Cited by 927
Chemical Fixation of Enzymes to Cyanogen Halide Activated Polysaccharide Carriers
Axéan, R., & Ernback, S. (1971) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1971.tb01250.x · Cited by 541
Johnson, R. R., Narvaez, J., An, G., & Ryan, C. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.24.9871 · Cited by 538
The proteinase inhibitors of plants and micro-organisms
Richardson, M. (1977) · Phytochemistry · doi:10.1016/s0031-9422(00)86777-1 · Cited by 282
Ryan, C. A. (1989) · BioEssays · doi:10.1002/bies.950100106 · Cited by 181
Research works printed but not linked: 3
- Li HS, Obak: Major soluble proteins of sweet potato roots and change in proteins after cutting, infection or storage. Agric Biol Chem 49: 733–744 (1985).
- Lin YH, Tsu BS: Some factors affecting levels of trypsin inhibitor activity of sweet potato (Ipomoea batatas Lam.) root. Bot Bull Acad Sin 28: 139–149 (1987).
- Yeh KW, Juan RH, Su JC: A rapid and efficient method for RNA isolation from plants with high carbohydrate content. Focus 13: 102–103 (1991).
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'Radicle' biochemistry: the biology of root-specific metabolism
Flores, H. (1999) · Trends in Plant Science · doi:10.1016/s1360-1385(99)01411-9 · Cited by 312
Shewry, P. R. (2003) · Annals of Botany · doi:10.1093/aob/mcg084 · Cited by 291
The Impact of Plant-Parasitic Nematodes on Agriculture and Methods of Control
Bernard, G. C., Egnin, M., & Bonsi, C. K. (2017) · InTech eBooks · doi:10.5772/intechopen.68958 · Cited by 245
Arabidopsis Vegetative Storage Protein Is an Anti-Insect Acid Phosphatase
Liu, Y., Ahn, J., Datta, S., Salzman, R. A., Moon, J., Huyghues‐Despointes, B. M. P., Pittendrigh, B. R., Murdock, L. L., Koiwa, H., & Zhu‐Salzman, K. (2005) · PLANT PHYSIOLOGY · doi:10.1104/pp.105.066837 · Cited by 201
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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- CoChat. (2026). Citation check: Functional activity of sporamin from sweet potato (Ipomoea batatas Lam.): a tuber storage protein with trypsin inhibitory activity. https://app.cochat.ai/papers/10.1023/a:1005764702510
- The paper
- Yeh, K.-W., Chen, J.-C., Lin, M.-I., Chen, Y.-M., & Lin, C.-Y. (1997). Functional activity of sporamin from sweet potato (Ipomoea batatas Lam.): a tuber storage protein with trypsin inhibitory activity. Plant Molecular Biology. https://doi.org/10.1023/a%3A1005764702510