The amino-acid sequence of the double-headed proteinase inhibitor from fox (Vulpes vulpes) submandibular glands.
Fox submandibular glands contain a double-headed secretory proteinase inhibitor. Its amino acid sequence was determined. Extensive homologies were found between this inhibitor and the corresponding inhibitors of cat, lion and dog in both domains. As in dog inhibitor the trypsin-inhibiting domain of fox inhibitor contains an Arg residue in the reactive site in contrast to a Lys residue in the inhibitors of cat and lion. Domains I and II of fox inhibitor are structurally related both to the sequenced inhibitors of cat, lion and dog and to the sequenced monovalent secretory pancreatic trypsin inhibitors. In comparison to cat and lion inhibitors the N-terminally extended sequences of fox and dog inhibitors seem to be characteristic for the inhibitor of Canidae.
Reisinger
P W
PW
Biochemisches Labor, Universität München, Federal Republic of Germany.
Hochstrasser
K
K
Wachter
E
E
D000595:Amino Acid Sequence; D000818:Animals; D005589:Foxes; D010455:Peptides / Q000302:isolation & purification; D011480:Protease Inhibitors / Q000032:analysis*; D013363:Submandibular Gland / Q000032:analysis*
D010455:Peptides; D011480:Protease Inhibitors