Dear Sir. Concerning your issue about the main sources to check alpha glucosidase inhibitory activity. inhibition of 𝛼-glucosidase is a useful treatment to delay the absorption of glucose after meals. As a megabiodiversity country, Indonesia still has a lot of potential unexploited forests to be developed as a medicine source, including as the 𝛼-glucosidase inhibitor. In this study, we determine the 𝛼-glucosidase inhibitory activity of 80% ethanol extracts of leaves and twigs of some plants from the Apocynaceae, Clusiaceae, Euphorbiaceae, and Rubiaceae. Inhibitory activity test of the 𝛼-glucosidase was performed in vitro using spectrophotometric methods. Compared with the control acarbose (IC50 117.20 μg/mL), thirty-seven samples of forty-five were shown to be more potent 𝛼-glucosidase inhibitors with IC50 values in the range 2.33–112.02 μg/mL. I think the following below links may help you in your analysis:

https://www.hindawi.com/journals/bmri/2012/281078/

http://www.phcogj.com/sites/default/files/10.5530pj.2017.3.60.pdf

https://www.ncbi.nlm.nih.gov/pubmed/26408887

http://www.academicjournals.org/journal/AJPP/article-full-text-pdf/709CD0262496

Thanks

My comment to Dr Isam Eldin Hussein Elgailani

in the first of the cited papers all the Lineawever Burk plots are incorrect becasue the plots are not linear!!!

It means that the enzyme exhibits positive cooperativity (No 1) or negative cooperativity (next plot) and no one of the constants: Km, kcat are proper.

Second comment: IC50 is not a constants at all; it is dependent on enzyme concentration. the constant is Ki.

Dear Minoli,

I am doing it in Acanthamoeba, and it is an evolutionary conserved enzyme so they could act as controls when doing mammalian study.

Best,

Mannan