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Pregled bibliografske jedinice broj: 202213

Purification and characterization of L, (L/D)-aminopeptidase from guinea pig serum


Krstanović, Marina; Brgles, Marija; Halassy, Beata; Frkanec, Ruža; Vrdoljak, Anto; Branović, Karmen; Benedetti, Fabio; Tomašić, Jelka
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.


Citiraj ovu publikaciju:

Krstanović, Marina; Brgles, Marija; Halassy, Beata; Frkanec, Ruža; Vrdoljak, Anto; Branović, Karmen; Benedetti, Fabio; Tomašić, Jelka
Purification and characterization of L, (L/D)-aminopeptidase from guinea pig serum // Preparative biochemistry & biotechnology, 36 (2006), 2; 175-195 (međunarodna recenzija, članak, znanstveni)
Krstanović, M., Brgles, M., Halassy, B., Frkanec, R., Vrdoljak, A., Branović, K., Benedetti, F. & Tomašić, J. (2006) Purification and characterization of L, (L/D)-aminopeptidase from guinea pig serum. Preparative biochemistry & biotechnology, 36 (2), 175-195.
@article{article, author = {Krstanovi\'{c}, Marina and Brgles, Marija and Halassy, Beata and Frkanec, Ru\v{z}a and Vrdoljak, Anto and Branovi\'{c}, Karmen and Benedetti, Fabio and Toma\v{s}i\'{c}, Jelka}, year = {2006}, pages = {175-195}, keywords = {L, (L/D)-aminopeptidase, N-acetylmuramyl-L-alanine amidase (EC 3.5.1.28), peptidoglycan monomer, guinea pig serum, mammalian sera}, journal = {Preparative biochemistry and biotechnology}, volume = {36}, number = {2}, issn = {1082-6068}, title = {Purification and characterization of L, (L/D)-aminopeptidase from guinea pig serum}, keyword = {L, (L/D)-aminopeptidase, N-acetylmuramyl-L-alanine amidase (EC 3.5.1.28), peptidoglycan monomer, guinea pig serum, mammalian sera} }
@article{article, author = {Krstanovi\'{c}, Marina and Brgles, Marija and Halassy, Beata and Frkanec, Ru\v{z}a and Vrdoljak, Anto and Branovi\'{c}, Karmen and Benedetti, Fabio and Toma\v{s}i\'{c}, Jelka}, year = {2006}, pages = {175-195}, keywords = {L, (L/D)-aminopeptidase, N-acetylmuramyl-L-alanine amidase (EC 3.5.1.28), peptidoglycan monomer, guinea pig serum, mammalian sera}, journal = {Preparative biochemistry and biotechnology}, volume = {36}, number = {2}, issn = {1082-6068}, title = {Purification and characterization of L, (L/D)-aminopeptidase from guinea pig serum}, keyword = {L, (L/D)-aminopeptidase, N-acetylmuramyl-L-alanine amidase (EC 3.5.1.28), peptidoglycan monomer, guinea pig serum, mammalian sera} }

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





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