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Title: | Preparation and properties of recombinant rat and human procholecystokinin(57-95). | Austin Authors: | Friedrich, Susann;Sims, Yulia;Baldwin, Graham S | Affiliation: | Department of Surgery, Austin Health, University of Melbourne, Heidelberg, VIC 3084, Australia | Issue Date: | 1-Apr-2008 | Publication information: | The Protein Journal; 27(3): 186-91 | Abstract: | Recombinant human progastrin(6-80) binds two ferric ions with an apparent dissociation constant of 2.2 +/- 0.1 microM [Baldwin (2004) Protein J 23:65-70]. The aims of the present study were to express fragments of recombinant procholecystokinin and to determine whether or not they bound ferric ions. Recombinant rat and human procholecystokinin(57-95) were expressed as glutathione S-transferase fusion proteins in E. coli. The fusion proteins were bound to glutathione-agarose, cleaved with thrombin, and purified by reverse phase HPLC. Recombinant procholecystokinin(57-95) did not bind to either the CCK1 or CCK2 receptor with high affinity. No change in absorption spectrum was observed on addition of ferric ions, and analysis of the quenching of tryptophan fluorescence observed in the presence of ferric ions indicated that binding to procholecystokinin(57-95) was at least 40-fold weaker than the binding of ferric ions to progastrin(6-80). | Gov't Doc #: | 18066654 | URI: | https://ahro.austin.org.au/austinjspui/handle/1/10478 | DOI: | 10.1007/s10930-007-9122-z | Journal: | The protein journal | URL: | https://pubmed.ncbi.nlm.nih.gov/18066654 | Type: | Journal Article | Subjects: | Amino Acid Sequence Animals Binding Sites Cholecystokinin.chemistry.genetics.isolation & purification.metabolism Ferric Compounds.metabolism Gene Expression Humans Kinetics Molecular Sequence Data Protein Binding Protein Precursors.chemistry.genetics.isolation & purification.metabolism Rats Receptors, Cholecystokinin.metabolism Recombinant Fusion Proteins.chemistry.genetics.isolation & purification.metabolism Sequence Homology, Amino Acid |
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