Separation of various calmodulins, calmodulin tryptic fragments, and different homologous Ca2+-binding proteins by reversed-phase, hydrophobic interaction, and ion-exchange high-performance liquid chromatography techniques.
Reversed-phase, hydrophobic interaction, and ion-exchange high-performance liquid chromatography techniques have been used to separate different Ca2+-binding proteins and their proteolytic fragments. An alkali-stable ion-exchange column permitted the baseline separation of calmodulin fragments which differed only by one to three charged amino acids. The new hydrophobic interaction chromatography system displayed a high-resolution power separating calmodulins from different sources and calmodulin fragments obtained by trypsin proteolysis. The properties and advantages of the different systems are discussed in detail.
D000818:Animals; D017317:Annexin A6; D001923:Brain Chemistry; D002118:Calcium; D002135:Calcium-Binding Proteins / Q000302:isolation & purification*; D002147:Calmodulin / Q000302:isolation & purification*; D002417:Cattle; D002851:Chromatography, High Pressure Liquid / Q000379:methods; D002852:Chromatography, Ion Exchange; D006868:Hydrolysis; D010446:Peptide Fragments / Q000302:isolation & purification*; D014357:Trypsin
D017317:Annexin A6; D002135:Calcium-Binding Proteins; D002147:Calmodulin; D010446:Peptide Fragments; D014357:Trypsin; D002118:Calcium