title: [Determination of the secondary prothrombin structure under different degrees of citraconylation by means of ring dichroism].
abstract: A process of spontaneous activation of bovine prothrombin under acylation of cytacone anhydride is studied by means of ring dichroism and disc electrophoresis in sodium dodecylsulphate. Ring dichroism data have shown that native prothrombin contains 14% of alpha-helical structures, 36% of beta-structures and 50% of random coil. Cytraconylation results in a fragmentation of native prothrombin chain and is accompanies by the decrease of alpha-helical regions in the fragments formed. Poly-L-lysine, modified by citracone anydride, does not form alpha-helical regions.
mesh_terms: D055598:Chemical Phenomena; D002621:Chemistry; D002942:Circular Dichroism; D004789:Enzyme Activation; D008298:Maleates; D010446:Peptide Fragments; D011107:Polylysine; D011487:Protein Conformation; D011516:Prothrombin
chemical_list: D008298:Maleates; D010446:Peptide Fragments; D011107:Polylysine; D011516:Prothrombin
vernacular_title: Opredelenie metodom krugovogo dikhroizma vtorichnoĭ struktury protrombina pri raznoĭ stepeni tsitrakonilirovaniia