A comparative study has been made of the β‐amylases of barley, wheat, rye, oats and sweet‐potato by means of exclusion chromatography and immunochemical analysis. The reactivity of barley malt and wheat β‐amylase was compared with different anti‐barley and anti‐wheat sera. In exclusion chromatography on Sephadex G100, barley β‐amylase yielded four, and both wheat and rye, two active components, whereas oat and sweet‐potato had only one active component. During the storage of barley, wheat and rye β‐amylases the large‐molecule components were split into smaller ones; no changes occurred in oat and sweet‐potato β‐amylases. On analysis against a specific barley β‐amylase antiserum, wheat and rye β‐amylase gave a reaction which indicated that they were immunologically partly identical with barley β‐amylase, and identical with each other. This serum induced no reaction in β‐amylases of sweet‐potato and oats. The rye β‐amylase precipitation line did not display enzymic activity after reaction with this antiserum. Analyses with different antisera of barley and wheat confirmed the partial immunological identity of barley malt and wheat β‐amylase. With some barley antisera, partial inhibition of wheat β‐amylase activity was observed. A similar phenomenon was apparent when barley malt β‐amylase was precipitated with some wheat antisera.
An amylase, previously detected in barley and described as a new barley amylase, has been further purified by immuno-affinity and ion exchange chromatography on CMcellulose. Analysis by isoelectricfocusing and immunochemical techniques showed that the enzyme preparation did not contain the normal a-and P-amylases usually found in barley and malt. The enzyme had a very low isoelectric point (ca pH 3.0) and was identified as an a-amylase on the basis of its action pattern on amylose.
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