Volume 72, Issue 4 pp. 360-365
Free Access

STUDIES ON CARBOHYDRATE-METABOLIZING ENZYMES. PART XIV. THE SPECIFICITY OF R-ENZYME FROM MALTED BARLEY*

D. J. Manners

D. J. Manners

Heriot-Watt University, Edinburgh

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Karen L. Sparra

Karen L. Sparra

Heriot-Watt University, Edinburgh

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First published: July‐August 1966
Citations: 23

Part XIII: Hutson, D. H., & Manners, D. J., Biochem. J., 1965, 94, 783.

Abstract

R-Enzyme and limit dextrinase of malted barley have been separated by continuous electrophoresis. The preparation of R-enzyme, which was free of α-amylase, hydrolysed the outermost inter-chain linkages of amylopectin and glycogen which had interior chain lengths exceeding five glucose residues. It had no action on glycogen with shorter interior chains, on pullulan, or on oligosaccharides containing α-1, 6-glucosidic linkages.

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