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Immobilization of neuraminidase and its potential application in the modification of cell surfaces

ER Bazarian and LB Wingard

Vibrio cholerae neuraminidase was immobilized on the inside of 1.0 mm inner diameter nylon tubing with retention of enzyme activity, when assayed at 37 degrees C and pH 5.5 with mucin as substrate. The stabilities of the immobilized and soluble enzymes were similar for up to 3 hr at 37 degrees C. Preliminary data indicated that immobilized neuraminidase will release sialic acid from the surface of leukemic AKR mouse thymus and spleen lymphocytes; however, the level of immobilized enzyme activity needs to be increased for practical applications. With this improvement immobilized neuraminidase could become a novel preparation for carrying out cell surface modifications with minimal enzyme contamination of the cell.

Volume 27, Issue 1, pp. 125-127, 01/01/1979
Copyright © 1979 by The Histochemical Society


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The Journal of Histochemistry & Cytochemistry is owned, published, and licensed by The Histochemical Society © 1979