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Preparation and Purification of Glucanase and Chitinase from Bean Leaves ¹

^a Plant Sciences Laboratories and United States Army Medical Research Institute of Infectious Diseases, Fort Detrick, Frederick, Maryland 21701

Glucanase (endo--1, 3-glucan 3-glucanohydrolase, EC 3.2.1.6, laminarinase, callase) and chitinase (poly--1, 4-[2-acetamido-2-deoxy] -D-glucoside glycanohydrolase, EC 3.2.1.14) were extracted from ethylene-treated bean (Phaseolus vulgaris L. cv. Red Kidney) leaves and purified on hydroxyapatite and carboxymethyl Sephadex columns. The glucanase prepared was homogeneous as judged by analytical centrifugation data, electrophoresis, and antibody-antigen reactions. On the basis of gel filtration, antibody-antigen reactions, and amino acid analysis, the molecular weight was estimated to be between 11,500 and 12,500. However, ultracentrifugation gave a higher estimate of 34,000. The glucanase had an isoelectric point near pH 11 and was specific for -1, 3-linkages. The chitinase was only partially purified as judged by electrophoretic behavior.

¹ In conducting the research reported herein, the investigators adhered to "Guide for Laboratory Animal Facilities and Care" established by the committee on the guide for laboratory animal facilities and care of the Institute of Laboratory Animal Resources, NAS-NRC.

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