The results on the investigations of the topography of the OSCP from b
ovine heart mitochondria are shortly reviewed. Hydrolysis of OSCP from
pig heart mitochondria by proteinase from Staphylococcus aureus and h
ydrolysis of the preliminary citraconylated OSCP by trypsin were folow
ed by isolation of the individual peptides by means of HPLC. Structura
l analysis of these peptides allowed us to reconstruct the complete am
ino acid sequence of this protein. Comparative structural analysis rev
ealed existence of the close homology (93.2%) between the pig OSCP and
the bovine OSCP. Some amino acid substitutions are localized close to
linear antigenic determinants of these proteins, or even within the a
mino acid sequence or some determinants.