Pregled bibliografske jedinice broj: 202213
Purification and characterization of L, (L/D)-aminopeptidase from guinea pig serum
Purification and characterization of L, (L/D)-aminopeptidase from guinea pig serum // Preparative biochemistry & biotechnology, 36 (2006), 2; 175-195 (međunarodna recenzija, članak, znanstveni)
CROSBI ID: 202213 Za ispravke kontaktirajte CROSBI podršku putem web obrasca
Naslov
Purification and characterization of L, (L/D)-aminopeptidase from guinea pig serum
Autori
Krstanović, Marina ; Brgles, Marija ; Halassy, Beata ; Frkanec, Ruža ; Vrdoljak, Anto ; Branović, Karmen ; Benedetti, Fabio ; Tomašić, Jelka
Izvornik
Preparative biochemistry & biotechnology (1082-6068) 36
(2006), 2;
175-195
Vrsta, podvrsta i kategorija rada
Radovi u časopisima, članak, znanstveni
Ključne riječi
L; (L/D)-aminopeptidase; N-acetylmuramyl-L-alanine amidase (EC 3.5.1.28); peptidoglycan monomer; guinea pig serum; mammalian sera
Sažetak
Mammalian sera contain enzymes that catalyze the hydrolytic degradation of peptidoglycans and molecules of related structure and are relevant for the metabolism of peptidoglycans. We now report on a novel L, (L/D)-aminopeptidase found in human and mammalian sera. The enzyme hydrolyses the pentapeptide L-Ala-D-iso-Gln-meso-DAP( NH2)-D-Ala-D-Ala yielding the free L-alanine and the respective tetrapeptide (KM 18 mM). L, (L/D)-aminopeptidase from guinea pig serum was highly purified in four chromatographic steps up to 700-fold. Molecular weight of the enzyme was estimated by HPLC to be approximately 175000. The configuration of alanine obtained by hydrolysis of the pentapeptide was determined by oxidation with L-amino acid oxidase. The amino acids sequence in the respective tetrapeptide was deduced from the results of mass spectrometry. The novel L, (L/D)-aminopeptidase also hydrolyzed alanine-4-nitroanilide (KM =0.6 mM) and several peptides comprising L-amino acids. Peptides containing D-amino acid at the amino end and L-Asp-L-Asp were not the substrates for this enzyme. The purified enzyme also exhibited enkephalin-degrading activity hydrolyzing enkephalins comprising L, L- and L, D-peptide bonds. The enzyme was inhibited strongly by metal-chelating agents, bestatin and amastatin.
Izvorni jezik
Engleski
Znanstvena područja
Kemija, Biologija, Temeljne medicinske znanosti
POVEZANOST RADA
Projekti:
0021002
Ustanove:
Imunološki zavod d.d.
Profili:
Ruža Frkanec
(autor)
Karmen Branović-Čakanić
(autor)
Jelka Tomašić
(autor)
Beata Halassy
(autor)
Marija Brgles
(autor)
Marina Krstanović
(autor)
Anto Vrdoljak
(autor)
Citiraj ovu publikaciju:
Časopis indeksira:
- Current Contents Connect (CCC)
- Web of Science Core Collection (WoSCC)
- Science Citation Index Expanded (SCI-EXP)
- SCI-EXP, SSCI i/ili A&HCI
- Scopus
- MEDLINE