L.S. Samokhina - Ph.D. (Biol.), Junior Research Scientist, A.N.Bach Institute of Biochemistry RAS (Moscow). E-mail: 6423918@mail.ru
I.I. Ionova - Ph.D. (Eng.), Associate Professor, Moscow State University of Food Production. E-mail: inna-ionova@yandex.ru
G.S. Komolova - Dr.Sc. (Biol.), Professor, A.N.Bach Institute of Biochemistry RAS (Moscow). E-mail: KomolovaGS@yandex.ru

Bioactive peptide complex marked as IVLF was isolated from bovine lactoferrin by pepsin hydrolysis. Mass spectrometric researches showed, that the complex consists of 7 peptides with molecular weight less than 3kDa. Their length doesn-t exceed 18 amino acid residues. Pepsin hydrolysate of the lactoferrin obtained from bovine milk possesses antimicrobial, bifidogenic, antioxidant, anti-ulcer qualities, which are more effective than in native lactoferrin. We identified peptide with high level of redox-active amino acid residues (Tyr, Trp, Met, Cys, His), that determine lactoferrin and it-shydrolysates antioxidant activity. Amino acid sequences analysis comparing to lactoferrin proteolysis Insilico modeling with Peptide Cutter program indicates that IVLF complex peptides can be predicted in most cases.The question of possible ways of increasing lactoferrin functional domens bioactivity while proteolysis is discussing. There is a reason of considering perspective of using IVLF peptide complex as an active base of medical and preventative measures in virtue of received data.