Bioscience, Biotechnology, and Biochemistry
Online ISSN : 1347-6947
Print ISSN : 0916-8451
Biochemistry & Molecular Biology Notes
Improvement in Performance of Affinity Gels Containing Gly-D-Phe as a Ligand to Thermolysin Due to Increasing the Spacer Chain Length
Kuniyo INOUYEKoji NAKAMURAMasayuki KUSANOKiyoshi YASUKAWA
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2007 Volume 71 Issue 8 Pages 2083-2086

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Abstract

The aim of this study was to improve the performance of affinity gels containing glycyl-D-phenylalanine (Gly-D-Phe) as a ligand to thermolysin. Gly-D-Phe was immobilized to the resin through spacers of varying chain lengths. The resulting affinity gels had spacer chain lengths of 2 carbon atoms and 11 and 13 carbon-and-oxygen atoms (designated T2, T11, and T13), and were characterized for their binding abilities to thermolysin. Measurement of adsorption isotherms showed that the association constants to thermolysin were in the order T13 > T11 > T2. In affinity column chromatography, in which 5 mg thermolysin was applied onto 1-ml volumes of the gels, the adsorption ratios of thermolysin were also in the order T13 > T11 > T2. These results indicate that the performance of affinity gels is improved by increasing the spacer chain length to 13 carbon-and-oxygen atoms.

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© 2007 by Japan Society for Bioscience, Biotechnology, and Agrochemistry
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