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

Edward R. Bazarian | Zendy; Lemuel B. Wingard | Zendy

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

Author(s) -

Edward R. Bazarian,

Lemuel B. Wingard

Publication year - 1979

Publication title -

journal of histochemistry and cytochemistry

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.971

H-Index - 124

eISSN - 1551-5044

pISSN - 0022-1554

DOI - 10.1177/27.1.35566

Subject(s) - neuraminidase , enzyme , sialic acid , immobilized enzyme , chemistry , vibrio cholerae , substrate (aquarium) , cell , biochemistry , neuraminic acid , surface modification , chromatography , biology , bacteria , ecology , genetics

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.

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