PMID: 2508551Oct 1, 1989Paper

Influence of lectin concentration on the catalytic properties of S1 nuclease bound to Concanavalin A-sepharose

Applied Biochemistry and Biotechnology
L G Reddy, V Shankar

Abstract

Partially purified S1 nuclease was bound through its carbohydrate moiety to Con A-Sepharose containing increasing amounts of lectin. The retention of activity was high, varying essentially from 75% on the "low lectin" matrix (1 mg Con A/mL of Sepharose), to no detectable activity on the "high lectin" matrix (8 mg Con A/mL of Sepharose). However, approximately 50% activity could be restored in "high lectin" matrix when the coupling was carried out in the presence of glucose, suggesting that the loss of activity on the "high lectin" matrix is caused by conformational changes brought about by the multiple attachment of the enzyme to the matrix. Interaction of Con A with S1 nuclease was used to predict the nature of carbohydrate moiety and its location with respect to the active site of the enzyme. Immobilization resulted in an increase in the optimum temperature, pH, and temperature stabilities, but it did not affect the pH optimum. A marginal increase in the apparent Km was observed. The bound enzyme also showed enhanced stability toward 8 M urea. On repeated use, the bound enzyme retained more than 80% of its initial activity after 6 cycles. These results are discussed taking into consideration the factors affecting immobilized ...Continue Reading

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Citations

Apr 1, 1991·Enzyme and Microbial Technology·M Saleemuddin, Q Husain
Mar 1, 1993·Enzyme and Microbial Technology·P MichalonC Marion
Jun 13, 2006·Biochimica Et Biophysica Acta·Kalyani MondalMunishwar Nath Gupta
Feb 15, 2003·FEMS Microbiology Reviews·Neelam A Desai, Vepatu Shankar
Jan 1, 1995·Critical Reviews in Microbiology·S U Gite, V Shankar
Jan 1, 1993·Critical Reviews in Biotechnology·L G Reddy, V Shankar
Mar 11, 2003·Biomacromolecules·Shweta SharmaMunishwar N Gupta

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