منابع مشابه
Evaluation of thrombolytic potential of three medicinal plants available in Bangladesh, as a potent source of thrombolytic compounds
Objective: The present study is aimed to investigate in vitro thrombolytic activity of three Bangladeshi medicinal plants Averrhoa bilimbi (Oxalidiaceae), Clerodendrum viscosum (Verbanaceae) and Drynaria quercifolia (Polypodiaceae). Materials and methods: Each the plant was extracted with methanol at room temperature and the concentrated methanolic extracts (MEF) were fractionated by the modifi...
متن کاملNatto and Its Active Ingredient Nattokinase A Potent and Safe Thrombolytic Agent
N atto is a traditional Japanese food made by boiling or steaming soybeans and fermenting them with the Bacillus subtilis natto. The bacillus bacteria activate a fermenting process that lends the beans their notoriously sour aroma, nutty flavor, and slippery texture. The Bacillus subtilis natto is a rod-shaped bacterium with a relatively high heat tolerance. Compared to other bacteria that have...
متن کاملNatural peptides and proteins: potent tyrosinase inhibitors
Background and objectives: Tyrosinase is a copper containing oxidase which is crucial for controlling the production of melanin in creatures such as bacteria, fungi, plants and mammals. It is involved in the first two steps of melanin biosynthesis and leads to pigmentation and different types of cancer such as melanoma. Also, it is responsible for browning of fruits and vegetab...
متن کاملStreptokinase--a clinically useful thrombolytic agent.
A failure of hemostasis and consequent formation of blood clots in the circulatory system can produce severe outcomes such as stroke and myocardial infraction. Pathological development of blood clots requires clinical intervention with fibrinolytic agents such as urokinase, tissue plasminogen activator and streptokinase. This review deals with streptokinase as a clinically important and cost-ef...
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ژورنال
عنوان ژورنال: International Current Pharmaceutical Journal
سال: 2012
ISSN: 2224-9486
DOI: 10.3329/icpj.v1i12.12454