N-(p-Aminophenyl)oxamic acid agarose is used in affinity chromatography, protein chromatography and in specialty resins. N-(p-Aminophenyl)oxamic acid has been used in studies characterizing sialidase, neuraminidase, β-N-acetylhexosaminidases and β-galactosidase.
Three beta-N-acetylhexosaminidases [EC 3.2.1.52] and one beta-galactosidase [EC 3.2.1.23] were purified from the culture filtrate of streptococcus 6646 group K by a combination of column chromatographies on p-aminophenyl beta-D-thiogalactopyranoside-substituted Sepharose and N-(paminophenyl)oxamic acid-substituted Sepharose. These beta-N-acetylhexosaminidases showed optimal activities between
European journal of biochemistry, 221(2), 655-664 (1994-04-15)
Sialidase activities of rabbit blood cells and serum were measured. The leucocyte particulate fraction showed the highest specific activity of sialidase towards mixed gangliosides and sialyllactose, and the cytosolic fraction showed for fetuin. Predominant sialidase activity in the blood was
The Journal of biological chemistry, 258(20), 12465-12471 (1983-10-25)
The naturally occurring sialic acids can have different types of N- and O-substitutions, resulting in more than 20 known isomers and compounds. Most methods for the detailed study of these various sialic acids require that the molecules be first released
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