Two major aminopeptidases, an aminopeptidase B and an aminopeptidase M-like enzyme, were purified from human skeletal muscle by DEAE-cellulose, HPLC gel filtration, and hydroxyapatite column chromatographies. The purified aminopeptidase B exhibits a molecular weight of 76,000 under both native and denaturing conditions. The activity of the aminopeptidase B is regulated by C1 ions and other anions in vitro. On the other hand, the aminopeptidase M-like enzyme is a monomeric protein having a molecular weight of 96,000. It is capable of significantly cleaving Phe-, Leu-, Arg-, and Ala-aminoacyl bonds in the presence of 2-mercaptoethanol. The pH optima for both enzymes are around 7.0, and bestatin is an effective inhibitor of both enzymes.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1093/oxfordjournals.jbchem.a122140 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Characterisation of Haemonchus contortus-derived cell populations propagated in vitro in a tissue culture environment and their potential to induce protective immunity in sheep.
Int J Parasitol
April 2001
Veterinary Pharmacology Research Laboratory, Veterinary Research Program, College of Veterinary Medicine, Mississippi State University 39762, Mississippi, MS, USA.
Cell populations derived from viable Haemonchus contortus L(3) larvae were propagated in vitro in a tissue culture environment for a prolonged period (>48 months). Microscopic evaluation of H. contortus-derived cell populations revealed gross morphological characteristics highly analogous to those described for cell types originating from species of plant nematodes propagated in vitro in a tissue culture environment for a briefer period of time (<6 months).
View Article and Find Full Text PDFBackground: Since kinins kallidin (KD) and bradykinin (BK) appear to have cardioprotective effects ranging from improved hemodynamics to antiproliferative effects, inhibition of kinin-degrading enzymes should potentiate such effects. Indeed, it is believed that this mechanism is partly responsible for the beneficial effects of angiotensin-converting enzyme (ACE) inhibitors. In the heart, enzymes other than ACE may contribute to local degradation of kinins.
View Article and Find Full Text PDFAcetaldehyde inhibits serum aminopeptidases.
Alcohol
October 1996
Department of Chemistry, Bowling Green State University, OH 43403, USA.
Aminopeptidase A (APA)- and aminopeptidase M (APM)-like activity were assayed in Moni-Trol ES with L-alpha-aspartyl-beta-naphthylamide and L-alanyl-beta-naphthylamide, respectively. Upon preincubation of the serum with 89.4, 223.
View Article and Find Full Text PDFTwo major aminopeptidases, an aminopeptidase B and an aminopeptidase M-like enzyme, were purified from human skeletal muscle by DEAE-cellulose, HPLC gel filtration, and hydroxyapatite column chromatographies. The purified aminopeptidase B exhibits a molecular weight of 76,000 under both native and denaturing conditions. The activity of the aminopeptidase B is regulated by C1 ions and other anions in vitro.
View Article and Find Full Text PDFSpectrum of cysteine peptide hydrolases was studied in human kidney cortex using a variety of protein and synthetic substrates after the preparation was fractionated on Sephadex G-100 following the precipitation with ammonium sulfate 40-70%. Activities of dipeptidyl aminopeptidase I, lysosomal carboxypeptidases A and B, cathepsins B and H, as well as the activity of Ca+2-dependent neutral proteinase were detected. A thiol-dependent proteolytic activity, which was apparently stimulated by cathepsin T- and -M like enzymes, was also observed.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!