The amino acid sequence of a trypsin inhibitor from the seeds of <i>Momordica charantia</i> Linn. Cucurbitaceae

Zeng, Fu‐Yue; Qian, Rui-Qing; Wang, Yu

doi:10.1016/0014-5793(88)81297-3

Cited by 15 publications

(3 citation statements)

References 9 publications

(10 reference statements)

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“…Bitter gourd seeds are known to contain a total of four trypsin inhibitors as well as four elastase inhibitors that belong to the squash family. Besides these, presence of one trypsin inhibitor each belonging to the Bowman‐Birk, Kunitz and potato inhibitor I family has also been reported in bitter gourd seeds (Zeng et al ., 1988). However, these PIs were suspected to be cultivar‐specific as they were not detected in the later studies (Hamato et al ., 1995).…”

Section: Introductionmentioning

confidence: 99%

Momordica charantia trypsin inhibitor II inhibits growth and development of Helicoverpa armigera

et al. 2009

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Bitter gourd (Momordica charantia L.) seeds contain several squash-type serine proteinase inhibitors (PIs), which inhibit the digestive proteinases of the polyphagous insect pest Helicoverpa armigera. In the present work isolation of a DNA sequence encoding the mature peptide of a trypsin inhibitor McTI-II, its cloning and expression as a recombinant protein using Pichia pastoris have been reported. Recombinant McTI-II inhibited bovine trypsin at 1 : 1 molar ratio, as expected, but did not inhibit chymotrypsin or elastase. McTI-II also strongly inhibited trypsin-like proteinases (81% inhibition) as well as the total proteolytic activity of digestive proteinases (70% inhibition) from the midgut of H. armigera larvae. The insect larvae fed with McTI-II-incorporated artificial diet suffered over 70% reduction in the average larval weight after 12 days of feeding. Moreover, ingestion of McTI-II resulted in 23% mortality in the larval population. The strong antimetabolic activity of McTI-II toward H. armigera indicates its probable use in developing insect tolerance in susceptible plants.

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Section: Introductionmentioning

confidence: 99%

Momordica charantia trypsin inhibitor II inhibits growth and development of Helicoverpa armigera

et al. 2009

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“…Homologous proteins with inhibitory properties against serine endopeptidases with a range of specificities have been subsequently characterized. Members of the family include inhibitors from other higher plants: tomato (Plunkett et al 1982;Wingate et al 1989), barley and millet (Svendsen et al 1980(Svendsen et al , 1982Tashiro et al 1991) adzuki and fava beans (Nozawa et al 1989;Svendsen et al 1984), and cucurbits (Zeng et al 1988;Krishnamoorthi et al 1990;Ogata et al 1991); and from an animal, the leech (Seemuller et al 1980). There have been suggestions that the proteinase B inhibitors from yeast (Maier et al 1979;Schu et al 1991) are also members of the family.…”

Section: Introductionmentioning

confidence: 99%

Evolution of the proteinase inhibitor I family and apparent lack of hypervariability in the proteinase contact loop

1994

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A protein phylogenetic tree was constructed from 24 homologous proteinase inhibitor I sequences identified in the EMBL/Genbank and Swiss-Prot databases and from translated amino acid data from four constitutive cDNA clones of proteinase inhibitor I characterized from potato tuber mRNA. The tree suggests that divergence of at least four paralogous proteins with functional specialization occurred at different times during the evolutionary history of the proteinase inhibitor I family. Five distinct regions in the primary structure, earlier identified by structural studies, were used to analyze the inhibitor family for hypervariability (Creighton and Darby, Trends Biochem Sci 14:319-324, 1989). Mutations did not occur with higher-than-random frequency within the proteinase binding region. When isoinhibitor, orthologous, or paralogous data subsets were subsequently analyzed the same results were obtained. Comparison of the amino acid sequences for all the known potato proteinase isoinhibitor I proteins identified ten highly variable sites. These also were distributed randomly. Thus hypervariability, which has been observed in all other serine proteinase inhibitor families to date, appears to be lacking in the proteinase inhibitor I family.

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“…3) have been isolated (Zeng et al, 1988) and range ia size from 62 to 77 amino adds, with 0 to 7 disulfide bridges. MCI-3 has no cysteine residues and is homologous to members of the Potato I inhibitor family.…”

Section: Three Trypsin Inhibitors From Momordica Charantia (Mci-1 MCmentioning

confidence: 99%

Structure-function study of a plant protein proteinase inhibitor: site-directed mutagenesis of Cucurbita maxima trypsin inhibitor V

Benavente

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The amino acid sequence of a trypsin inhibitor from the seeds of Momordica charantia Linn. Cucurbitaceae

Cited by 15 publications

References 9 publications

Momordica charantia trypsin inhibitor II inhibits growth and development of Helicoverpa armigera

Momordica charantia trypsin inhibitor II inhibits growth and development of Helicoverpa armigera

Evolution of the proteinase inhibitor I family and apparent lack of hypervariability in the proteinase contact loop

Structure-function study of a plant protein proteinase inhibitor: site-directed mutagenesis of Cucurbita maxima trypsin inhibitor V

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