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The major androgen‐dependent protease in dog prostate belongs to the kallikrein family: confirmation by partial amino acid sequencing
Author(s) -
Lazure C.,
Leduc R.,
Seidah N.G.,
Chrétien M.,
Dubé J.Y.,
Chapdelaine P.,
Frenette G.,
Paquin R.,
Tremblay R.R.
Publication year - 1984
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(84)80557-8
Subject(s) - autolysis (biology) , kallikrein , amino acid , biochemistry , proteases , peptide sequence , protease , biology , esterase , homology (biology) , serine , enzyme , chemistry , microbiology and biotechnology , gene
Canine prostate fluids and seminal plasma contain a major androgen‐dependent protein which was identified as a proteolytic enzyme exhibiting an Arg‐esterase activity. This protease, as characterized, is shown to be present as a two‐chain structure held together by at least one disulfide bridge and composed of approximately 220 amino acids. Amino acid sequence determination of both chains has revealed a clear homology to other known amino acid sequences of serine proteases. Furthermore, the comparison of the presented 58 amino acids of the Arg‐esterase with the other sequences revealed a very strong homology (larger than 50%) to members of the kallikrein family. The two chain structure could thus result from autolysis of a single chain enzyme in the ‘kallikrein autolysis loop’. Amino acid composition of the canine prostatic enzyme suggests that it is related, but not identical, to pancreatic canine kallikrein.