Grebenshchikova O G, Alekseeva A E, Potapkina T A, Kozin S A, Dedinskiĭ I R, Prozorovskiĭ V N
Biokhimiia. 1994 May;59(5):694-702.
The structural and functional peculiarites of alcohol dehydrogenases (ADH) of some biological species have been studied using antipeptide antibodies (AB). The synthetic peptides were used which corresponded to the functionally important sites (1-14, 93-115, 265-276) of equine liver ADH. Conjugates of peptides with protein carriers were obtained and used for immunization of laboratory animals. It was shown that the antipeptide antibodies formed therefrom could interact with the corresponding synthetic peptides, with conjugates derived from them as well as with the native enzyme. The results of cross-reactivity of antipeptide AB with ADH from other biological sources suggest that amino acid sequences (1-14), (93-115) and (265-276) contain common antigenic determinants for the corresponding ADH from animal sources. According to computer prediction data for linear epitopes of equine liver ADH, sequence (93-115) comprises amino acid residues of the antigenic determinants with enhanced conformational rigidity which is consistent with the literary data on the functional significance of this site (the loop ligating the second Zn atom). Sequences (1-14) and (265-276) contain amino acid residues capable of interacting with AB and pertaining, in all probability, to antigenic determinants formed by mobile structures.
