Aminopeptidase-B in the rat testes: isolation, functional properties and cellular localization in the seminiferous tubules.

@article{Cadel1995AminopeptidaseBIT,
  title={Aminopeptidase-B in the rat testes: isolation, functional properties and cellular localization in the seminiferous tubules.},
  author={Sandrine Cadel and Adrian R Pierotti and Thierry Foulon and Christophe Cr{\'e}minon and Nicole M Barr{\'e} and Dominique Segretain and Paul Cohen},
  journal={Molecular and cellular endocrinology},
  year={1995},
  volume={110 1-2},
  pages={149-60}
}
An aminopeptidase of the B-type, with an apparent M(r) 72,000 and pI = 4.9, was isolated from rat testes and characterized. The enzyme was able to remove only Arg and/or Lys residues from L-amino acid beta-naphthylamide derivatives and from the N-terminus of several peptides. No cleavage occurred in the case of Arg-Pro bonds as found in bradykinin and substance P. The enzyme was sensitive to cysteinyl reagents and to aminopeptidase inhibitors, such as bestatin, amastatin and arphamenines A and… CONTINUE READING
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