Literature DB >> 6445824

Sheep liver beta-N-acetylhexosaminidase: partial purification, characterization and photodynamic inactivation.

L A Donoso, J D Spikes.   

Abstract

Sheep liver beta-N-acetylhexosaminidase was purified over 20-fold by conventional methods. The enzyme possessed activity against both p-nitrophenly-beta-D-N-acetylglucosaminide and p-nitrophenyl-beta-D-N-acetylgalactosaminide as substrates. On the basis of a variety of physical and chemical analyses including pH stability, substrate inhibition studies and photodynamic inactivation, it was concluded that both the beta-N-acetylglucosaminidase and beta-N-acetylgalactosaminidase activities reside within the same molecule.

Entities:  

Mesh:

Substances:

Year:  1980        PMID: 6445824     DOI: 10.1159/000459229

Source DB:  PubMed          Journal:  Enzyme        ISSN: 0013-9432


  3 in total

1.  Isolation and photo-oxidation of lysozyme fragments.

Authors:  I Ferrer; E Silva
Journal:  Radiat Environ Biophys       Date:  1981       Impact factor: 1.925

2.  Photooxidative changes of lysozyme with 337.1 nm laser radiation.

Authors:  D L VanderMeulen; M M Judy
Journal:  Radiat Environ Biophys       Date:  1988       Impact factor: 1.925

3.  Generating high quality libraries for DIA MS with empirically corrected peptide predictions.

Authors:  Brian C Searle; Kristian E Swearingen; Christopher A Barnes; Tobias Schmidt; Siegfried Gessulat; Bernhard Küster; Mathias Wilhelm
Journal:  Nat Commun       Date:  2020-03-25       Impact factor: 14.919

  3 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.