[Polypeptide serine proteinase inhibitors isolated from venom from several reptilian species].
The survey encompasses literature data on the polypeptide inhibitors of some reptiles serine proteinases and their separation from adder Viperidae and cobra Elapidae species. The evolutionary comparison of physico-chemical and biological properties of them are also given and discussed within this work. Considerable homology (about 50%) in amino acid composition of adder, bee, mammal and others of different phylogenetic origin is being emphasized and high homology in structure of their functionally important inhibitors sites is observed. In the most cases the investigated peptide inhibitors of adder and cobra were observed to have an extremely high antitryptic activity with Ki ranging from 7.6 x 10(-10) M to 3.5 x 10(-12) M. The majority of polypeptide inhibitors are suggested by Laskowsky et al to interact with the proteinases in a standard way. The biological reactivity of the above preparations is a result of arginine and lysine presence in the substrate-binding sites of P2' and P3' or P4' centres.
Kolodzeĭskaia
M V
MV
A. V. Palladin Institute of Biochemistry, National Academy of Science of Ukraine, Kyiv. Chernish@biochem.ua
D000595:Amino Acid Sequence; D000818:Animals; D002853:Chromatography, Liquid / Q000379:methods; D004591:Electrophoresis, Polyacrylamide Gel; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry / Q000302:isolation & purification* / Q000494:pharmacology; D017386:Sequence Homology, Amino Acid; D015842:Serine Proteinase Inhibitors / Q000737:chemistry / Q000302:isolation & purification* / Q000494:pharmacology; D013045:Species Specificity; D017819:Viperidae
D010455:Peptides; D015842:Serine Proteinase Inhibitors