Biochemical characterisation of a Kunitz-type inhibitor from Tamarindus indica L. seeds and its efficacy in reducing plasma leptin in an experimental model of obesity

被引：29

作者：

de Medeiros, Amanda Fernandes ^{[1
]}

Costa, Izael de Sousa ^{[1
]}

Coimbra de Carvalho, Fabiana Maria ^{[1
]}

Kiyota, Sumika ^{[2
]}

Pinheiro de Souza, Beatriz Blenda ^{[3
,4
]}

Sifuentes, Daniel Nogoceke ^{[4
]}

Serquiz, Raphael Paschoal ^{[1
]}

Lima Maciel, Bruna Leal ^{[5
,6
]}

Uchoa, Adriana Ferreira ^{[1
,7
]}

dos Santos, Elizeu Antunes ^{[1
,8
]}

de Araujo Morais, Ana Heloneida ^{[1
,6
]}

机构：

[1] Univ Fed Rio Grande do Norte, Biosci Ctr, Postgrad Biochem Program, Natal, RN, Brazil

[2] CPDSA, Inst Biol, Lab Prot & Peptide Biochem, Sao Paulo, Brazil

[3] Univ Brasilia, Inst Biol Sci, Postgrad Biol Mol, Brasilia, DF, Brazil

[4] EMBRAPA, Embrapa Genet Resources & Biotechnol, Brasilia, DF, Brazil

[5] Univ Fed Rio Grande do Norte, Postgrad Nutr Program, Ctr Hlth Sci, Natal, RN, Brazil

[6] Univ Fed Rio Grande do Norte, Dept Nutr, Ctr Hlth Sci, Natal, RN, Brazil

[7] Univ Fed Rio Grande do Norte, Dept Cell Biol & Genet, Biosci Ctr, Natal, RN, Brazil

[8] Univ Fed Rio Grande do Norte, Dept Biochem, Biosci Ctr, Natal, RN, Brazil

来源：

JOURNAL OF ENZYME INHIBITION AND MEDICINAL CHEMISTRY | 2018年 / 33卷 / 01期

关键词：

Tamarind; antitryptic; Wistar rats; CCK; TRYPSIN-INHIBITOR; PROTEASE INHIBITORS; FOOD-INTAKE; WEIGHT; PURIFICATION; ANTIOXIDANT; RESISTANCE; PHYSIOLOGY; SECRETION; RELEASE;

D O I：

10.1080/14756366.2017.1419220

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

A trypsin inhibitor isolated from tamarind seed (TTI) has satietogenic effects in animals, increasing the cholecystokinin (CCK) in eutrophy and reducing leptin in obesity. We purified TTI (pTTI), characterised, and observed its effect upon CCK and leptin in obese Wistar rats. By HPLC, and after amplification of resolution, two protein fractions were observed: Fr1 and Fr2, with average mass of [M +14H](+) = 19,594,690 Da and [M + 13H](+) = 19,578,266 Da, respectively. The protein fractions showed 54 and 53 amino acid residues with the same sequence. pTTI presented resistance to temperature and pH variations; IC50 was 2.7 x 10(-10) mol.L-1 and Ki was 2.9 x 10(-11) moL(-1). The 2-DE revealed spots with isoelectric points between pH 5 and 6, and one near pH 8. pTTI action on leptin decrease was confirmed. We conclude that pTTI is a Kunitz trypsin inhibitor with possible biotechnological health-related application.

引用

页码：334 / 348

页数：15

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