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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
DOI: 10.1007/s10930-007-9122-z
Journal: The protein journal
Type: Journal Article
Subjects: Amino Acid Sequence
Binding Sites
Cholecystokinin.chemistry.genetics.isolation & purification.metabolism
Ferric Compounds.metabolism
Gene Expression
Molecular Sequence Data
Protein Binding
Protein Precursors.chemistry.genetics.isolation & purification.metabolism
Receptors, Cholecystokinin.metabolism
Recombinant Fusion Proteins.chemistry.genetics.isolation & purification.metabolism
Sequence Homology, Amino Acid
Appears in Collections:Journal articles

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