Results 151 to 160 of about 804,350 (314)

In Vitro Inhibition of α-Amylase and α-Glucosidase by Different Parts of Amla Plant (Phyllanthus emblica L)

Pharmacology and Clinical Pharmacy Research, 2018
Amla plant (Phyllanthus emblica L) has been empirically used to treat diabetes. The aim of this study was to determine the most potential part of amla plant that can be used as α-glucosidase and α-amylase inhibitors.
Novi I. Fauzi, Maria Ulfah, Syarif Hamdani, Saeful Hidayat   +3 more
doaj  

Cloning, molecular characterization and heterologous expression of AMY1, an α-amylase gene from Cryptococcus flavus [PDF]

FEMS Microbiology Letters, 2008
Alexsandro S. Galdino, Cirano J. Ulhoa, Lídia Maria P. Moraes, Maura V. Prates, Carlos Bloch, Fernando A.G. Torres   +5 more
openaire   +1 more source

Amylase activity of von Ebner's glands during feeding in rats

, 1992
P(論文)To evaluate the physiological role of von Ebner's glands, changes of amylase activity in the glands before and after feeding were compared with the amylase activity of parotid glands, submandibular glands, sublingual glands, the pancreas and plasma.
小原, 伸子, 星, 和明, 武田, 正子, 倉橋, 昌司, 23200, 猪股, 孝四郎, 23201, 23202, 23203, 23204, 23205, 鈴木, 光代   +11 more
core  

Photooxidation of Hog Pancreatic α Amylase

, 1970
The findings suggest that histidine is present at the "active site" of hog pancreatic a amylase. The functions of α and β amylase are explained.
Edward A. Sweeney, R. Bruce Donoff
core   +1 more source

Bio‐guided fractionation of (9Z)‐5,8,11‐trihydroxyoctadec‐9‐enoic acid from Abelmoschus sagittifolius root as a potent α‐glucosidase inhibitor: An integrated in vitro and in silico study

Journal of the Science of Food and Agriculture, EarlyView.
Abstract BACKGROUND Abelmoschus sagittifolius stands out as a valuable medicinal source for developing functional food targeting type 2 diabetes. This study investigated the α‐glucosidase inhibitory potential of an active fraction obtained from A. sagittifolius roots (ASR), enriched in (9Z)‐5,8,11‐trihydroxyoctadec‐9‐enoic acid (OA), using both enzyme ...
Nguyen Phuong Mai, Nguyen Van Quan, Nguyen Dang Duc, Tran Dang Xuan   +3 more
wiley   +1 more source

Evaluation of alpha- amylase inhibition by Urtica dioica and Juglans regia extracts [PDF]

Iranian Journal of Basic Medical Sciences, 2014
Objective(s):One strategy for the treatment of diabetes is inhibition of pancreatic α- amylase. Plants contains different chemical constituents with potential for inhibition of α-amylase and hence maybe used as therapeutic.
Mahsa Rahimzadeh, Samaneh Jahanshahi, Soheila Moein, Mahmood Reza Moein   +3 more
doaj  

Catalytic and Thermodynamic Properties of Digitaria exilis β-amylase

Journal of Plant Sciences, 2006
Ayodele O. Kolawole, David M. Sanni ., Joshua O. Ajele .   +2 more
openaire   +1 more source

High-Resolution α‑Amylase Assay Combined with High-Performance Liquid Chromatography–Solid-Phase Extraction–Nuclear Magnetic Resonance Spectroscopy for Expedited Identification of α‑Amylase Inhibitors: Proof of Concept and α‑Amylase Inhibitor in Cinnamon

, 2016
Type 2 diabetes affects millions of people worldwide, and new improved drugs or functional foods containing selective α-amylase inhibitors are needed for improved management of blood glucose.
Dan Staerk (135389), Kenneth T. Kongstad (1647898), Anna K. Jäger (1647889), Leyla Okutan (2124982)   +3 more
core   +1 more source

Exocrine Gland Dysfunction in Parkinson's Disease: Pathophysiology, Clinical Manifestations, and Therapeutic Perspectives—A Narrative Review

Movement Disorders Clinical Practice, EarlyView.
Abstract Background Non‐motor symptoms, especially autonomic dysfunction, are major contributors to disability and decreased quality of life in Parkinson's disease (PD). Despite being common and having a wide range of clinical facets, exocrine gland dysfunction is still not well recognized and managed.
Renato P. Munhoz, Marina Farah, Laura Silveira‐Moriyama   +2 more
wiley   +1 more source

Detection of residual α-amylase in the concentrated PB product.

, 2015
(a) One-microliter of protein extract from 2 mg of concentrated PB product was subjected to immunoblot analysis (five independently prepared samples). The α-amylase level in each signal was estimated by comparison with standards (2.5, 5.0, 10, and 25 ng)
Masaru Ohta (703001), Kenji Sekikawa (703003), Makoto Takano (371653), Hidenori Takagi (702997), Lijun Yang (356935), Noriko Kitamura (702999), Yoshihiro Fujiwara (80708), Shimpei Hayashi (385420), Takachika Hiroi (69958), Fumio Takaiwa (685566), Yuhya Wakasa (702996), Nobumasa Watanabe (702998), Kenjirou Ozawa (703004), Yuko Ogo (703000), Wai Wai Thet Tin (703002)   +14 more
core   +1 more source