New ligands for human C-reactive protein: calcium-dependent binding with epsilon-aminocaproic acid-agarose and calcium-independent binding with omega-aminohexyl-agarose.
Human C-reactive protein (CRP) is an acute phase protein which increases in concentration in response to inflammation. CRP has been known to bind with phosphorylcholine in a calcium-dependent manner. In this study, CRP is found to bind to affinity chromatography of negatively-charged epsilon-aminocaproic acid-agarose when calcium ions are present, and to the affinity chromatography of positively-charged omega-aminohexyl-agarose if a normal ionic strength of NaCl exists but calcium ion is not present.
Department of Laboratory Medicine, Osaka City University Medical School, Japan.
S
S
Kuwajima
T
T
Kishida
T
T
Noda
Y
Y
Izumi
K
K
Naka
T
T
Matsui
K
K
Okuda
D000614:Aminocaproates; D015119:Aminocaproic Acid / Q000378:metabolism; D002097:C-Reactive Protein / Q000378:metabolism*; D002118:Calcium / Q000502:physiology*; D002846:Chromatography, Affinity; D006801:Humans; D008024:Ligands; D011485:Protein Binding; D012685:Sepharose / Q000031:analogs & derivatives* / Q000378:metabolism
D000614:Aminocaproates; D008024:Ligands; C024903:aminohexyl-sepharose; D002097:C-Reactive Protein; D012685:Sepharose; D002118:Calcium; D015119:Aminocaproic Acid