Primary structure of a Kunitz-type trypsin inhibitor from Enterolobium contortisiliquum seeds

Batista, Isabel de Fátima Correia; Oliva, Maria Luíza Vilela; Araújo, Magali; Sampaio, Misako U.; Richardson, Michael; Fritz, Hans; Sampaio, Cláudio Hoffmann

doi:10.1016/0031-9422(95)00710-5

Cited by 99 publications

(105 citation statements)

References 18 publications

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“…6.5% as the ApTI isoinhibitors represent 7.0% of this fraction. These data are in agreement with other protease inhibitors purified from Leguminosae seeds, like EcTI (12%) from Enterolobium contortisiliquum, (Batista et al, 1996); AeTI (8.0%) from Archidendron ellipticum, (Bhattacharyya et al, 2006); BvcTI (4.1%) and BvlTI (8.5%) from Bauhinia variegata candida and lilac (Ciero et al, 1996), respectively. The homogeneity of these fractions was checked by SDS-electrophoresis, as showed in Fig.…”

Section: Purificationsupporting

confidence: 86%

“…as for other inhibitors described from the Mimosoideae (Batista et al, 1996;Oliva et al, 2000;Vargas et al, 2004). In agreement with these data, mass spectrometry analyses were measured from the SEC samples, as they indicated the presence of three isoforms with the following molecular mass : 19,709 Da,19,869 and 20,378 Da (data not shown).…”

Section: Structural Characterizationmentioning

confidence: 78%

“…The presence of protease inhibitors isoforms in plant seeds is commonly reported, but the characterization of all of them is rarely performed (Bhattacharyya et al, 2006;Batista et al, 1996;Morrison et al, 2007).…”

Section: Purificationmentioning

confidence: 99%

“…contortisiliquum trypsin inhibitor) (Batista et al, 1996) for trypsin (1.56 nM) and a-chymotrypsin (120 nM).…”

Section: Binding Constantsmentioning

confidence: 99%

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Physico-chemical and antifungal properties of protease inhibitors from Acacia plumosa

et al. 2009

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Section: Purificationsupporting

confidence: 86%

Section: Structural Characterizationmentioning

confidence: 78%

Section: Purificationmentioning

confidence: 99%

“…contortisiliquum trypsin inhibitor) (Batista et al, 1996) for trypsin (1.56 nM) and a-chymotrypsin (120 nM).…”

Section: Binding Constantsmentioning

confidence: 99%

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Physico-chemical and antifungal properties of protease inhibitors from Acacia plumosa

et al. 2009

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“…Members of this subfamily have been found in a variety of botanical families, however most research has been directed to inhibitors of the three legume subfamilies (Fabaceae family). Inhibitors of the Papilionoideae and Caesalpinioideae subfamilies usually have a polypeptide chain while inhibitors from the Mimosoideae subfamily consist of two polypeptide chains joined by disulfide bridges, being characterized as dimeric proteins (Batista et al, 1996;Norioka et al, 1988). The presence of carbohydrates is a common feature for inhibitors of the Kunitz family; however, there are few reports on the structural aspects.…”

Section: Serine Protease Inhibitorsmentioning

confidence: 99%

Affinity Chromatography as a Key Tool to Purify Protein Protease Inhibitors from Plants

Santos¹,

Oliveira²,

Rabêlo³

et al. 2012

Affinity Chromatography

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New small proteinase inhibitors from Capsicum annuum seeds: Characterization, stability, spectroscopic analysis and a cDNA cloning

et al. 2013

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Recent results from our laboratory have previously shown the purification of a small serine proteinase inhibitor (PI), named CaTI1, from Capsicum annuum seeds. This work demonstrated the characterization of CaTI now named CaTI1, and the identification of two other small serine PIs, named CaTI2 and CaTI3, also present in these seeds. CaTI1 presented molecular mass of 6 kDa and pI value of ∼9.0. CaTI1 inhibited both trypsin and chymotrypsin with inhibition constants (Ki and Ki') of 14 and 2.8 nM for trypsin and 4.3 and 0.58 nM for chymotrypsin, respectively. Circular dichroism analysis suggested the predominance of both disordered and β-strands regions in the secondary structure. CaTI1 presented striking physico-chemical stability. In an attempt to get the entire sequence of CaTI1 we found another PI called CaTI2. The discussion of this finding is in the main text. A degenerate primer was designed based on the sequence of trypsin inhibitor CaTI1 in an attempt to achieve the cloning of this PI. Surprisingly, the alignment of the predicted peptide derived from the cDNA with the protein database showed similarity with other C. annuun PIs, and thus it was called CaTI3.

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Primary structure of a Kunitz-type trypsin inhibitor from Enterolobium contortisiliquum seeds

Cited by 99 publications

References 18 publications

Physico-chemical and antifungal properties of protease inhibitors from Acacia plumosa

Physico-chemical and antifungal properties of protease inhibitors from Acacia plumosa

Affinity Chromatography as a Key Tool to Purify Protein Protease Inhibitors from Plants

New small proteinase inhibitors from Capsicum annuum seeds: Characterization, stability, spectroscopic analysis and a cDNA cloning

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