Abstract
In principle any ligand-binding site with an appreciable degree of specificity can be used to purify a macromolecule by affinity chromatography. We have prepared a resin which contains covalently bound tyrosyl groups and employed it to purify one enzyme (tyrosyl-tRNA synthetase from E. coli) which interacts with the resin via its substrate-binding site and another (DAHP synthetase from yeast) which interacts via an effector-binding site. Our resin which contains a hexamethylene diamine (HMD) extension between the agarose matrix and the ligand appears to bind DAHP synthetase much more strongly than the previously used “tyrosineSepharose” which lacked such a spacer (1).
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© 1974 Plenum Press, New York
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Gallopo, A.R., Kotsiopoulos, P.S., Mohr, S.C. (1974). Purification of Tyrosine-Sensitive 3-Deoxy-D-Arabinoheptulosonate-7-Phosphate (DAHP) and Tyrosyl-tRNA Synthetases on Agarose Carrying Carboxyl-Linked Tyrosine. In: Dunlap, R.B. (eds) Immobilized Biochemicals and Affinity Chromatography. Advances in Experimental Medicine and Biology, vol 42. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-6982-0_12
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DOI: https://doi.org/10.1007/978-1-4684-6982-0_12
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