Characterization of serological properties of polyclonal antibodies produced against enzymes involved in the L-selective cleavage of hydantoin derivatives |
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Authors: | Martin Siemann Christoph Syldatk Fritz Wagner |
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Institution: | (1) Institute of Biochemistry and Biotechnology, Technical University of Braunschweig, Konstantin-Uhde-Stae 5, 3300 Braunschweig, FRG |
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Abstract: | Summary Polyclonal antibodies were produced against the highly purified enzymes L-hydantoinase, hydantoin-racemase and L-N-carbamoylamino acid amidohydrolase of Arthrobacter aurescens DSM 3747. In order to exploit these antibodies for basic research (molecular biology) or bioengineering (process development), the serological properties had to be characterized. Both, the hydantoinase- and carbamoylase-antibodies were observed to be monofunctional, whereas the hydantoin-racemase-antibody was found to be additionally specific against the L-hydantoinase. Monospecificity was realized after affinity chromatography. Investigations on serological crossreactions with several linear- and cyclic amidases (e.g. hydantoinases) as well as hydantoin-racemases are demonstrated in this paper.Deticated to Prof. Dr. Klaus Mosbach on the occation of his 60th birthday. |
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