ISSN:
1573-9104
Keywords:
albumin inhibitors
;
α-amylase
;
affinity chromatography
;
Octopus vulgaris
;
Lam.
;
wheat flour
Source:
Springer Online Journal Archives 1860-2000
Topics:
Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
Notes:
Abstract Octopus α-amylase has been purified to homogeneity by single-step affinity chromatography on Sepharose-bound wheat albumin inhibitors. Two electrophoretically distinguishable isoamylases are obtained, both consisting of a single polypeptide chain with molecular weight 45,000. Octopus α-amylase is more effectively inhibited by a monomeric than by a dimeric protein inhibitor from wheat. The inhibition is dependent on pH, temperature, and time of preincubation. Properties are compared with those of other animal α-amylases.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF01093885
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