Zobrazeno 1 - 4
of 4
pro vyhledávání: '"Ludovica Faotto"'
Autor:
Severino Ronchi, Armando Negri, Gabriella Tedeschi, Ludovica Faotto, Fabrizio Ceciliani, Michele Mortarino, Tatjana Simonic
Publikováno v:
Scopus-Elsevier
L-Aspartate oxidase is a monomeric flavoprotein that catalyzes the first step in the de novo biosynthetic pathway for pyridine nucleotide formation under both aerobic and anaerobic conditions. In spite of the physiological importance of this biosynth
Publikováno v:
Biotechnology Letters. 17:193-198
The amino acid sequence of D-amino acid oxidase from Rhodotorula gracilis was determined by automated Edman degradation of peptides generated by enzymatic and chemical cleavage. The enzyme monomer contains 368 amino acid residues and its sequence is
The primary structure of a basic (pI 9.0) fatty acid-binding protein from liver of Gallus domesticus
Publikováno v:
Comparative biochemistry and physiology. Part B, Biochemistrymolecular biology. 109(2-3)
The complete amino acid sequence of a basic (pI 9.0) fatty acid-binding protein purified from liver of Gallus domesticus was determined by automated Edman degradation of tryptic, CNBr/HFBA and Staphylococcus aureus protease peptides. The protein cont
Autor:
Ludovica Faotto, Armando Negri, Severino Ronchi, Alberto Bartorelli, Bruno Berra, Irma Colombo, Fabrizio Ceciliani
Publikováno v:
FEBS Letters. (2-3):147-150
UK114 is a tumor antigen expressed by various malignant neoplasms. The complete amino acid sequence of UK114 purified from goat liver has been determined by automated Edman degradation of CNBr and endoproteinase Lys-C peptides. The protein contains 1