A Kunitz proteinase inhibitor from Archidendron ellipticum seeds: purification, characterization, and kinetic properties.

@article{Bhattacharyya2006AKP,
  title={A Kunitz proteinase inhibitor from Archidendron ellipticum seeds: purification, characterization, and kinetic properties.},
  author={Arindam Bhattacharyya and Suman Mazumdar and S. M. Leighton and Cherukuri R. Babu},
  journal={Phytochemistry},
  year={2006},
  volume={67 3},
  pages={
          232-41
        }
}
Physico-Chemical and Antifungal Properties of a Trypsin Inhibitor from the Roots of Pseudostellaria heterophylla
TLDR
Extended research on Pseudostellaria heterophylla proteins makes PHTI an exploitable candidate as an antifungal protein for further investigation, and shows it could inhibit the growth of the phytopathogens and Fusarium oxysporum through disruption of the cell membrane integrity.
Purification and characterization of a trypsin inhibitor from Plathymenia foliolosa seeds.
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PFTI showed significant inhibitory activity against trypsin-like proteases present in the larval midguts on A. kuehniella and D. saccharalis and could suppress the growth of larvae.
Purification and Characterization of a Novel Inhibitor from Poinciana pulcherrima Seeds with Activity towards Pest Digestive Enzymes
TLDR
The plant genes expressing such TIs can be isolated, cloned and introduced in vegetable crops, thereby conferring resistance and minimizing the devastating crop yield losses caused by various insect pests and pathogens.
Purification of a novel pepsin inhibitor from Coriolus versicolor and its biochemical properties.
TLDR
A novel pepsin inhibitor was isolated from Coriolus versicolor and differs from the reported aspartic protease inhibitors, according to the secondary structure and the kinetic studies of this inhibitor.
Purification, characterization and evaluation of insecticidal activity of trypsin inhibitor from Albizia lebbeck seeds
TLDR
The inhibitor was found to be susceptible to varying concentrations of reducing agents like DTT and 2-mercaptoethanol, thereby indicating the role of disulphide bridges in maintaining its three dimensional structure and stability and the sequence of the genes encoding for such inhibitors can be determined.
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References

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Acacia Proteinase Inhibitors
TLDR
Amo-terminal sequence analysis of the two polypeptide chains of the inhibitors revealed extensive homology with the trypsin inhibitor from the silk tree (another Mimosoideae legume); both these inhibitor are homologous with the soybean trypsIn inhibitor (Kunitz).
Proteinase inhibitors from a mimosoideae legume, Albizzia julibrissin. Homologues of soybean trypsin inhibitor (Kunitz).
TLDR
Four proteinase inhibitors were isolated from seeds of Albizzia julibrissin of the subfamily Mimosoideae, which is often regarded as the most primitive group of the Leguminosae plants, and revealed a considerable homology with soybean trypsin inhibitor (Kunitz).
The trypsin and chymotrypsin inhibitors in chick peas (Cicer arietinum L.). Purification and properties of the inhibitors.
TLDR
From a crude extract of chick peas, inhibitors of trypsin and chymotrypsin were isolated by affinity chromatography on a column oftrypsin-Sepharose 6B, indicating that they are mixtures of native and tryps inmodified forms and that they probably have separate sites for the two enzymes.
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