ISSN: 2573-4555

Традиционная медицина и клиническая натуропатия

Открытый доступ

Наша группа организует более 3000 глобальных конференций Ежегодные мероприятия в США, Европе и США. Азия при поддержке еще 1000 научных обществ и публикует более 700 Открытого доступа Журналы, в которых представлены более 50 000 выдающихся деятелей, авторитетных учёных, входящих в редколлегии.

 

Журналы открытого доступа набирают больше читателей и цитируемости
700 журналов и 15 000 000 читателей Каждый журнал получает более 25 000 читателей

Индексировано в
  • Индекс источника CAS (CASSI)
  • Google Scholar
  • Шерпа Ромео
  • Открыть J-ворота
  • Генамика ЖурналSeek
  • РефСик
  • Каталог индексирования исследовательских журналов (DRJI)
  • Университет Хамдарда
  • ЭБСКО, Аризона
  • Публикации
  • Женевский фонд медицинского образования и исследований
  • Евро Паб
  • ICMJE
Поделиться этой страницей

Абстрактный

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.