ISSN: 2573-4555

Medicina Tradicional e Naturopatia Clínica

Acesso livre

Nosso grupo organiza mais de 3.000 Séries de conferências Eventos todos os anos nos EUA, Europa e outros países. Ásia com o apoio de mais 1.000 Sociedades e publica mais de 700 Acesso aberto Periódicos que contém mais de 50.000 personalidades eminentes, cientistas de renome como membros do conselho editorial.

Periódicos de acesso aberto ganhando mais leitores e citações
700 periódicos e 15 milhões de leitores Cada periódico está obtendo mais de 25.000 leitores

Indexado em
  • Índice de Fonte CAS (CASSI)
  • Google Scholar
  • Sherpa Romeu
  • Abra o portão J
  • Genâmica JournalSeek
  • RefSeek
  • Diretório de indexação de periódicos de pesquisa (DRJI)
  • Universidade Hamdard
  • EBSCO AZ
  • Publons
  • Fundação de Genebra para Educação e Pesquisa Médica
  • Euro Pub
  • ICMJE
Compartilhe esta página

Abstrato

Identification of a Proteinaceous Alpha Amylase Inhibitor from a Medicinal Herb Oxalis corniculata L. (Oxalidaceae)

Jyothi KSN , Shailaja M, Viveni J and Suresh C

Health management through traditional medicine is a promising approach worldwide as it represents a multifaceted approach to health care than conventional medicine. The heightened importance to validate the efficacy and standards of traditional herbal medicine is the thrust area of present day research. The present study is one such attempt to evaluate the alpha amylase inhibitory potential and identify the candidate inhibitor from Oxalis corniculata L, a potent indigenous medicinal plant. Sequential solvent extraction of the leaves of O. corniculata was performed in previous work and the aqueous extract, showing maximum inhibition against porcine pancreatic alpha amylase against starch as substrate (IC50 value 68.08+0.06), was selected for purification using ammonium sulphate precipitation. The pellet obtained at 40%-80% precipitation was further subjected to ion exchange chromatography on DEAE-cellulose and gel filtration chromatography using Sephadex G-100. The molecular weight of the proposed amylase inhibitor named AI-1 was estimated to be about 30 kda on SDS-PAGE. Temperature sensitivity and pH stability of the inhibitor was studied. The AI-1 protein was stable up to 400 C and was totally destroyed beyond 700 C and showed maximum activity at pH 6. Further characterization of the AI-1 protein and its sequence determination will help in discovering a novel proteinaceous alpha amylase inhibitor from O. corniculata. Research of this kind will help to usher the identification of active bioconstituents from plants with great medicinal activities.