[Interrelation of conformational changes of crustacin and its capacity to bind specifically with carcino-embryonic antigen].
Temperature-, ionic strength-, calcium ion- and pH-dependence of spatial structure of crustacin have been studied using CD and fluorescent spectroscopy. Secondary structure of crustacin was estimated by CD spectra. An irreversible conformational transition of crustacin's protein moiety connected with the loss of CEA-binding activity has been found at ca. 50 degrees C. Crustacin is shown to be calcium-binding protein, stability of the native crustacin conformation being markedly enhanced by calcium ions (1 mM Ca2+ shifted up the transition temperature by approximately 10 degrees C). Calcium binding and ionic strength increase led to alteration of both secondary and tertiary structures of crustacin. The highest CEA-binding activity was observed for the calcium-bond form of crustacin. A lack of specific interaction of crustacin with some saccharides was shown. Interrelation between conformation and immunochemical activity of crustacin is discussed.
Glazunov
V P
VP
Tarankova
Z A
ZA
Odinokov
S E
SE
Kurika
A V
AV
Pavlenko
A F
AF
D002118:Calcium / Q000494:pharmacology; D002135:Calcium-Binding Proteins / Q000032:analysis* / Q000276:immunology; D002272:Carcinoembryonic Antigen / Q000032:analysis*; D002942:Circular Dichroism; D006863:Hydrogen-Ion Concentration; D037102:Lectins; D009994:Osmolar Concentration; D011487:Protein Conformation; D013050:Spectrometry, Fluorescence; D013696:Temperature
D002135:Calcium-Binding Proteins; D002272:Carcinoembryonic Antigen; D037102:Lectins; C060167:crustacin protein, Pagurus prideauxii; D002118:Calcium
Vzaimosviaz' konformatsionnykh izmeneniĭ krustatsina i ego sposobnosti spetsificheski sviazyvat'sia s rakovo-émbrional'nym antigenom.