PURIFICATION AND CHARACTERIZATION OF AN a-AMYLASE INHIBITOR FROM MAISE (ZEA MAIZE)
Por:
BLANCO-LABRA, A., ITURBE-CHIÑAS, F.A.
Publicada:
1 ene 1981
Resumen:
a-Amylase inhibitor is presented in maize seeds. It is a protein as indicated by precipitation with ammonium sulfate and trichloroacetic acid, denaturation by heat, digestion with proteases and by dye-staining. It was purified to homogeneity by ammonium sulfate precipitation and Sephadex G-75 gel filtration. It had an apparent molecular weight of 29,600 and did not contain any carbohydrate. Its properties differed from those of previously reported a-amylase inhibitors, since it was active against a-amylase of maize, produced during germination as well as against Bacillus subtilis a-amylase. It was also active against a-amylase from the insects Tribolium castaneum, Sitophilus zeamais and Rhyzopertha dominica, but it was inactive against a-amylase from human saliva, hog pancreas, Aspergillus oryzae, wheat, rye, barley, triticale, and sorghum. It was stable for 5 min at 96°C at pH 7. Maximal inhibition required at least 10 min of preincubation with the enzyme at pH 6.8 and 257deg;C. Polyacrylamide gel electrophoresis gave three protein bands, but only one was obtained in S.D.S. and mercaptoethanol. Copyright © 1981, Wiley Blackwell. All rights reserved
Filiaciones:
BLANCO-LABRA, A.:
Department of Biochemistry, (D.E.Pg.) School of Chemistry, Universidad Nacional Autónoma de México, Mexico
ITURBE-CHIÑAS, F.A.:
Department of Biochemistry, (D.E.Pg.) School of Chemistry, Universidad Nacional Autónoma de México, Mexico
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