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• W1965403721 abstract "The use of cyanogen bromide-activated Sepharose condensed with amines containing alkyl and ω-aminoalkyl groups has provided a series of columns for attempted purifications of the threonine-sensitive aspartokinase-homoserine dehydrogenase of Escherichia coli. Among the alkyl-substituted Sepharose derivatives (Sepharose ∼ NH-(CH2)XH), there was no retardation on the ethyl derivative, slight retardation on the propyl derivative, retardation over a broad band with low yield on the butyl derivative, and strong binding on the pentyl derivative from which active enzyme was not eluted by increased salt concentrations or by a number of other potential eluants. On the ω-aminoalkyl-substituted Sepharose derivatives (Sepharose ∼ NH-(CH2)X-NH2), there was observed no retention on the aminobutyl derivative, retardation with good purification on the aminohexyl and aminoheptyl derivatives, and strong binding on the aminononyl derivative from which active enzyme was not eluted by the several methods attempted. Thus, an appropriate functional group in addition to lengthening the hydrocarbon chain may be necessary for the success of this type of chromatography." @default.
• W1965403721 created "2016-06-24" @default.
• W1965403721 creator A5015850272 @default.
• W1965403721 creator A5059706221 @default.
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• W1965403721 date "1976-05-01" @default.
• W1965403721 modified "2023-10-17" @default.
• W1965403721 title "Purification of the threonine-sensitive aspartokinase-homoserine dehydrogenase complex using chromatography on substituted Sepharose columns" @default.
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• W1965403721 doi "https://doi.org/10.1016/0003-2697(76)90501-7" @default.
• W1965403721 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/782283" @default.
• W1965403721 hasPublicationYear "1976" @default.
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