title: Rapid purification of the 30 kDa calcimedin using DNase I affinity chromatography.
abstract: The 30 kDa calcimedin was found to bind directly to phenyl-Sepharose in a calcium dependent manner similar to calmodulin. The 30 kDa calcimedin was also found to bind to and inhibit DNase I. This calcium-dependent binding was exploited to develop a two-step purification scheme for this calcimedin. In addition, affinity-purified antibodies to the 30 kDa calcimedin were used to examine its tissue distribution. The highest levels were found in lung, trachea and diaphragm while the lowest levels of the 30 kDa calcimedin were found in brain and skeletal muscle.
authors.affiliation: Department of Physiology and Cell Biology, University of Texas Health Science Center, Houston 77025.
authors.forename: V L
authors.initials: VL
authors.lastname: Smith
authors.forename: J R
authors.initials: JR
authors.lastname: Dedman
mesh_terms: D000199:Actins / Q000378:metabolism; D000818:Animals; D017302:Annexins; D001667:Binding, Competitive; D002135:Calcium-Binding Proteins / Q000302:isolation & purification* / Q000378:metabolism; D002846:Chromatography, Affinity; D003850:Deoxyribonuclease I / Q000378:metabolism; D008970:Molecular Weight; D051381:Rats; D012685:Sepharose / Q000031:analogs & derivatives; D014018:Tissue Distribution
chemical_list: D000199:Actins; D017302:Annexins; D002135:Calcium-Binding Proteins; C020927:phenyl-sepharose; D012685:Sepharose; D003850:Deoxyribonuclease I