High impact information on BLMH

• In the current study, we cloned the cDNA for the catalytic subunit of chicken aminopeptidase H [1].
• Chicken aminopeptidase H is a cysteine protease possessing endopeptidase as well as aminopeptidase activity [Rhyu, M. R., Nishimura, T., Kato, Y., Okitani, A. & Kato, H. (1992) Eur. J. Biochem. 208, 53-59] [1].
• The open reading frame of the aminopeptidase H gene consists of 1362 base pairs encoding a 52-kDa protein consistent with the molecular mass determined on SDS/PAGE; the deduced amino acid sequence contains all the partial sequences determined for the purified enzyme [1].
• Purification and properties of aminopeptidase H from chicken skeletal muscle [2].
• Aminopeptidase H exhibits activity against both L-leucine beta-naphthylamide and alpha-N-benzoyl-DL-arginine beta-naphthylamide [2].

Associations of BLMH with chemical compounds

• Aminopeptidase H was purified from fresh chicken breast muscle by ammonium sulfate fractionation and successive chromatographies on DEAE-cellulose, Ultrogel AcA 34, activated thiol-Sepharose 4B, phenyl-Sepharose CL-4B and DEAE-cellulose again [2].

Analytical, diagnostic and therapeutic context of BLMH

• Furthermore, the expression of aminopeptidase H in COS7 cells was also recognized on immunoblotting [1].

References