Purification and properties of an alpha amylase inhibitor specific for human pancreatic amylase from proso panicum miliaceum seeds

Nagaraj, R.H.; Pattabiraman, T.N.

Journal of Biosciences 7(3-4): 257-268


ISSN/ISBN: 0250-5991
Accession: 006229234

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An .alpha.-amylase inhibitor was purified to homogeneity by acid extraction, ammonium sulphate fractionation, chromatography on carboxymethyl-cellulose, diethylaminoethyl-cellulose and Sephadex G-100 from proso grains (Panicum miliaceum). The calculated molecular weight was 14,000. The inhibitor was fairly heat stable under acidic and neutral conditions. The factor was more effective by two orders of magnitude in its action on human pancreatic amylase than on human salivary amylase, It did not inhibit on Aspergillus oryzae, Bacillus subtilis and porcine pancreatic amylases. Pepsin rapidly inactivated the inhibitor. Chemical modification studies revealed that amino and guanido groups are essential for the action of the inhibitor. The inhibitor was found to protect both human salivary and pancreatic amylases against inactivation by acid. The mode of inhibition was found to be uncompetitive.