Chemical Constituents from Caesalpinia sappan and Their Biological Activity | Chapter 7 | Novel Aspects on Chemistry and Biochemistry Vol. 5

 This study aims to judge the arginase inhibitory activity of unique compounds from Caesalpinia sappan L. heartwood. Based on bioactivity-guided fractionation, the ethyl acetate fraction (prevents arginase activity at a aggregation of 50 μg/mL) was further subjected to column chromatography to get five compounds (1-5). The chemical buildings of the isolated compounds were determined by resolving NMR spectral dossier and referring to data from the biography. The arginase II inhibitory activity of compounds 1-5 was examined in vitro utilizing an enzyme solution processed from the kidney of numb C57BL/6 mice. Compounds 1 and 5 potentially restrict arginase II activity, accompanying IC50 values of 8.1 and 12.6 μM, whereas the staying compounds were inactive. This study is the first to evaluate compounds isolated from C. sappan heartwood with regard to their arginase inhibitory exercise.

Author(s) Details:

Dao-Cuong To,
Phenikaa University Nano Institute (PHENA), Phenikaa University, Yen Nghia, Ha Dong District, Hanoi 12116, Vietnam.

Le-Minh Hoang,
Phenikaa University Nano Institute (PHENA), Phenikaa University, Yen Nghia, Ha Dong District, Hanoi 12116, Vietnam.

Truong Thi Viet Hoa,
Phenikaa University Nano Institute (PHENA), Phenikaa University, Yen Nghia, Ha Dong District, Hanoi 12116, Vietnam.

Truong Thi Thuy Nhung ,
Phenikaa University Nano Institute (PHENA), Phenikaa University, Yen Nghia, Ha Dong District, Hanoi 12116, Vietnam.

Hoa-Thi Nguyen,
Phenikaa University Nano Institute (PHENA), Phenikaa University, Yen Nghia, Ha Dong District, Hanoi 12116, Vietnam.

Truong-Nhan Ngu,
Department of Natural Sciences and Technology, Tay Nguyen University, 567 Le Duan, Buon Ma Thuot, Dak Lak 630000, Vietnam.

Truong Ba Phong,
Department of Natural Sciences and Technology, Tay Nguyen University, 567 Le Duan, Buon Ma Thuot, Dak Lak 630000, Vietnam.

Van-Tinh Nguyen,
Applied Biomedical Research Institute, Buon Ma Thuot Medical University, 298 Ha Huy Tap Str., Buon Ma Thuot, Dak Lak 630000, Vietnam.

Please see the link here: https://stm.bookpi.org/NACB-V5/article/view/11580

Determining the Pancreatic Arginase Activity and α- Amylase Levels in Patients with Type 2 Diabetes and Alcoholic Pancreatitis | Chapter 2 | Challenging Issues on Environment and Earth Science Vol. 5

 Arginase, a regenerative enzyme found in the endocrine pancreas, participates in insulin metabolism as well as regenerative processes during polyamine formation. High levels of -amylase have been linked to pancreatic damage. The purpose of this study was to see how arginase and -amylase functioned in the pancreas of people with type 2 diabetes and those who had alcohol-induced acute pancreatitis. Arginase and -amylase activities in pancreatic tissue were measured in patients with type 2 diabetes mellitus or acute pancreatitis without pancreatic diabetes. The results were compared to those of a control group. Our findings show that diabetic pancreas has higher arginase activity than controls, whereas pancreatitis tissues have lower arginase activity (P 0.05). The activity of a-amylase was higher in the pancreas of type 2 diabetes patients than in the pancreas of acute pancreatitis patients. Rather than being a source of damage mediators, increased arginase activity in type 2 diabetes patients may be associated with an effort to reclaim endocrine pancreatic function. Because pancreatitis causes acinar damage, resulting in the release of a-amylase, this enzyme was found to be higher in diabetic pancreatic tissue than in nondiabetic pancreatic tissue.

Author (S) Details

José D. Méndez
Medical Research Unit in Metabolic Diseases, Cardiology Hospital, National Medical Center, Mexican Institute of Social Security, México.

Roberto De Haro
Medicine Section, Iztacala Faculty, National Autonomous University of Mexico, Los Reyes Iztacala, Tlalnepantla, State of Mexico, 54090, Mexico.

Verna Méndez-Valenzuela
General Hospital 49, Mexican Institute of Social Security, Los Moch, México.

Jorge L. Ble-Castillo
Research Station in DACS. Juárez Autonomous University of Tabasco, Avenida Gregorio Méndez 2890 Colonia Tamulte. 86100. Villahermosa, Tabasco, Mexico.

Hector O. Rubio
Faculty of Zootechnology and Ecology, Autonomous University of Chihuahua, Periferico Francisco R. Almada, Km 1, CP: 31453. Chihuahua, México.

View  Book :-  https://stm.bookpi.org/CIEES-V5/article/view/1826