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. Author manuscript; available in PMC: 2011 Apr 20.
Published in final edited form as: Biochemistry. 2010 Apr 20;49(15):3351–3365. doi: 10.1021/bi100198y

Figure 4.

Figure 4

Purification and characterization of AnaPS module 1. (A) Purity of the thioredoxin fusion protein of AnaPS module 1 (Trx-C*A1T1) post Ni-NTA chromatography and concentration-induced protein precipitation. Cartoon representation is used to indicate the identity and domain-composition of the two prominent bands present in the gel as determined by peptide mass fingerprinting. (B) ATP-[32P]PPi exchange assay data obtained for Trx-C*AT. 100% relative activity for anthranilate-dependent exchange corresponds to 6200 CPM. (C) Autoradiograph of SDS-PAGE gel illustrating the covalent loading of [carboxy-14C]anthranilate onto the holo-T-domain of Trx-C*AT.