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Selective Beta-N-acetylhexosaminidase from Aspergillus versicolor—a tool for producing bioactive carbohydrates

2019
Beta-N-Acetylhexosaminidases (EC 3.2.1.52) are typical of their dual activity encompassing both N-acetylglucosamine and N-acetylgalactosamine substrates. Here we present the isolation and characterization of a selective -N-acetylhexosaminidase from the fungal strain of Aspergillus versicolor.
Bojarová, P. (Pavla)   +7 more
openaire   +1 more source

Blood testosterone levels are correlated with beta-N-acetylhexosaminidase activity in human caput epididymis.

Biochemistry and molecular biology international, 1993
beta-N-acetylhexosaminidase exhibits a relatively high activity in human epididymis. Its isoenzymatic profile and immunological properties led us to conclude that the increased activity was not due to the expression of an isoform unrelated to the HEX A and B present in other human tissues.
A, Datti   +4 more
openaire   +1 more source

Beta-N-acetylhexosaminidase in the splen of a patient with hairy-cell leukaemia.

1990
he spleen from a patient with hairy-cell leukaemia had beta-N-acetylhexosaminidase activity that could be resolved into three isoenzymes by chromatography on phenyl boronate agarose. Two of these were the major forms, A and B, found in normal tissues but, in addition, there was an 'extra' form that accounted for 15% of total activity.
EMILIANI, Carla   +3 more
openaire   +1 more source

β-N-Acetylhexosaminidase in spinal muscular atrophy fibroblasts

Clinica Chimica Acta, 1993
TASSI, Carmelo   +3 more
openaire   +2 more sources

Beta-N-acetylhexosaminidase

1991
Dietmar Schomburg, Margit Salzmann
openaire   +1 more source

The beta-N-Acetylhexosaminidase in the Synthesis of Bioactive Glycans: Protein and Reaction Engineering

2019
N-Acetylhexosamine oligosaccharides terminated with GalNAc act as selective ligands of galectin-3, a biomedically important human lectin. Their synthesis can be accomplished by beta-N-acetylhexosaminidases (EC 3.2.1.52). Advantageously, these enzymes tolerate the presence of functional groups in the substrate molecule, such as the thiourea linker ...
Bojarová, P. (Pavla)   +5 more
openaire   +1 more source

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