Purification and partial characterization of a Schizolobium parahyba chymotrypsin inhibitor

Souza, Elizabeth Maria Talá de; Mizuta, Kumiko; Sampaio, Misako U.; Sampaio, Cláudio Hoffmann

doi:10.1016/0031-9422(94)00921-f

Cited by 33 publications

(20 citation statements)

References 17 publications

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“…After negative staining for inhibitor, only one protein band was detected in the gel with a strong inhibitory activity for trypsin. The isoelectric point of CPTI is 4.0, showing it to be an acid protein, and agrees with the isoelectric point found in the literature for most proteases inhibitors (19,20).…”

Section: Discussionsupporting

confidence: 89%

See 1 more Smart Citation

Isolation and Characterization of a New Trypsin Inhibitor from Crotalaria paulina Seeds

Pando

Ciero²,

Novello

et al. 1999

IUBMB Life

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SummaryA new trypsin inhibitor (CPTI) has been isolated from Crotalaria paulina seeds. Puri cation of the inhibitor was carried out by gel ltration, ion-exchange chromatography, and subsequent reversed-phase HPLC. The presence of a single polypeptide chain, with a molecular mass of 20 kDa and isoelectric point 4.0, was detected. The trypsin inhibitor had a K i value of 4.5 £ 10 ¡ 8 M and was capable of acting on human, bovine, and porcine trypsin and weakly on bovine chymotrypsin. Amino acid analysis showed that CPTI has a high content of aspartate, glutamate, leucine, serine, and glycine, having 177 amino acid residues in its composition. These data suggest that the protein belongs to the Kunitz-type trypsin inhibitors. IUBMB Life, 48: 519-523, 1999

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Section: Discussionsupporting

confidence: 89%

“…Given that Kunitztype inhibitors have one or two disul de bridges and given the apparent absence of free cysteines on the previously reported inhibitors (19,20), we assume that CPTI has one disul de bridge.…”

Section: Discussionmentioning

confidence: 99%

Isolation and Characterization of a New Trypsin Inhibitor from Crotalaria paulina Seeds

Pando

Ciero²,

Novello

et al. 1999

IUBMB Life

View full text Add to dashboard Cite

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“…Apart from very alkaline pH (>12) where AeTI lost $34% of its potency after 2 h and $65% after 4 h, extremes of pH had negligible effects on AeTI activity. The unusually high thermostability and high pH amplitude of AeTI has also been observed for other serine PIs, such as the chymotrypsin inhibitors isolated from Enterolobium contortisiliquum (Batista et al, 1996), Schizolobium parahyba (Souza et al, 1995) and Psophocarpus tetragonolobus (Gruen et al, 1984). Barring an initial fall of $20% inhibitory activity during the first three months, AeTI retained over 70% trypsin inhibition upon storage at À20°C for over a period of one year.…”

Section: Nomenclaturementioning

confidence: 88%

“…for PIs isolated from Enterolobium contortisiliquum (Batista et al, 1996), Schizolobium parahyba (Souza et al, 1995) and Glycine max (Freed and Ryan, 1980). The titration curve obtained with bovine trypsin suggests that 100% inhibition has not taken place.…”

Section: Kinetics Of Inhibition and Inhibition Constantmentioning

confidence: 89%

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

et al. 2006

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“…In recent studies, the herbal extract of S. parahyba leaves and fractions was shown to possess potent secondary metabolites that are able to inhibit local tissue damage, such as hemorrhage and myotoxicity induced by Bothrops snake venoms (Vale et al, 2007;Mendes et al, 2008). Other studies with this plant showed the isolation of serine proteinase inhibitors from its seeds (Mizuta and Ventura, 1976;Souza et al, 1995;Sampaio et al, 1996;Teles et al, 2004). In many countries, plant extracts are used traditionally in the treatment of snakebite envenomations.…”

Section: Introductionmentioning

confidence: 96%

Acute toxicity of Schizolobium parahyba aqueous extract in mice

Mendes¹,

Vale²,

Lucena³

et al. 2009

Phytotherapy Research

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The herbal extract of Schizolobium parahyba leaves is used commonly in the Brazil central region to treat snakebites. This study evaluates the acute toxicological effects of Schizolobium parahyba aqueous extract in mice 24 h after intraperitoneal administration. Acute toxicity was evaluated using biochemical, hematological and histopathological assays. Alterations in the levels of transaminases, bilirubin, albumin and prothrombrin time were observed, and these are likely to occur due to hepatic injury, which was confirmed by light microscopy. Liver histopathological analysis revealed the presence of lymph plasmocitary inflammatory infiltrate, but no other histopathological alterations were observed in any of the other organs analysed. The data confirm the low toxicity of the extract of Schizolobium parahyba and provide a model for the selection of a dose that does not cause injuries in the organism.

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Purification and partial characterization of a Schizolobium parahyba chymotrypsin inhibitor

Cited by 33 publications

References 17 publications

Isolation and Characterization of a New Trypsin Inhibitor from Crotalaria paulina Seeds

Isolation and Characterization of a New Trypsin Inhibitor from Crotalaria paulina Seeds

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

Acute toxicity of Schizolobium parahyba aqueous extract in mice

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