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E56h + E59h Mutation Affects Binding Of The Recombinant Haemphilus Influenza Carbonic Anhydrase To A Ni-Nta Column, Eric D. Lebel, Kathleen Cornely
E56h + E59h Mutation Affects Binding Of The Recombinant Haemphilus Influenza Carbonic Anhydrase To A Ni-Nta Column, Eric D. Lebel, Kathleen Cornely
Chemistry & Biochemistry Student Scholarship
The Haemophilus influenzae carbonic anhy- drase (HICA) is important in converting carbon dioxide to bicarbonate in bacteria. Endogenous cellular proteins, like Escherichia coli carbonic anhydrase (ECCA), have been observed to bind to a Ni-NTA column, which can be used as a means of protein purification. The possibility ex- ists that proteins that do not normally bind to Ni-NTA, like HICA, can be engineered using site directed mutagenesis to introduce histidine resi- dues that would give the protein the capability to bind, allowing for a one-step purification method. Site-directed mutagenesis was used to introduce the double mutation of E56H + E59H …
Mutation Of Surface Histidines In Haemophilus Influenzae Carbonic Anhydrase To Enable Purification By Metal Affinity Chromatography, Shelby E. Scola, Kathleen Cornely
Mutation Of Surface Histidines In Haemophilus Influenzae Carbonic Anhydrase To Enable Purification By Metal Affinity Chromatography, Shelby E. Scola, Kathleen Cornely
Chemistry & Biochemistry Student Scholarship
No abstract provided.