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Affinity chromatography of a regulatory enzyme based on specific interaction with the effector

Authors
Publisher
Elsevier Inc.
Publication Date
Volume
37
Issue
2
Identifiers
DOI: 10.1016/0006-291x(69)90730-x
Disciplines
  • Biology

Abstract

Abstract A crude extract of yeast was chromatographed on a column of Sepharose containing covalently bound L-tyrosine. The tyrosine-sensitive 3-deoxy-D- arabino -heptulosonate-7-phosphate (DAHP) synthetase was retarded by the column relative to the bulk of the protein and was purified about 100-fold. In contrast, the phenylalanine-sensitive enzyme was not retarded. No retardation was found on an unsubstituted Sepharose column. The purification presumably resulted from the specific interaction between the effector-binding site of the enzyme and the effector attached to Sepharose.

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