Literature DB >> 5482165

[Fluorescence study of Schiff bases of pyridoxal. Comparison with L-aspartate aminotransferase].

M Arrio-Dupont.   

Abstract

Entities:  

Mesh:

Substances:

Year:  1970        PMID: 5482165     DOI: 10.1111/j.1751-1097.1970.tb06062.x

Source DB:  PubMed          Journal:  Photochem Photobiol        ISSN: 0031-8655            Impact factor:   3.421


× No keyword cloud information.
  4 in total

1.  Molecular heterogeneity of O-acetylserine sulfhydrylase by two-photon excited fluorescence fluctuation spectroscopy.

Authors:  G Chirico; S Bettati; A Mozzarelli; Y Chen; J D Müller; E Gratton
Journal:  Biophys J       Date:  2001-04       Impact factor: 4.033

2.  Fluorescence of the Schiff bases of pyridoxal and pyridoxal 5'-phosphate withL-isoleucine in aqueous solutions.

Authors:  G Cambrón; J M Sevilla; T Pineda; M Blázquez
Journal:  J Fluoresc       Date:  1996-03       Impact factor: 2.217

3.  Characterization of C-S Lyase from C. diphtheriae: a possible target for new antimicrobial drugs.

Authors:  Alessandra Astegno; Alejandro Giorgetti; Alessandra Allegrini; Barbara Cellini; Paola Dominici
Journal:  Biomed Res Int       Date:  2013-09-11       Impact factor: 3.411

4.  Asymmetry of the active site loop conformation between subunits of glutamate-1-semialdehyde aminomutase in solution.

Authors:  Barbara Campanini; Stefano Bettati; Martino Luigi di Salvo; Andrea Mozzarelli; Roberto Contestabile
Journal:  Biomed Res Int       Date:  2013-07-31       Impact factor: 3.411

  4 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.