Characterization of human liver (4-methylumbelliferyl-α-d-N-acetylneuraminic acid) neuraminidase activity
| Autor: | Jack A. Alhadeff, Susan Wolfe |
|---|---|
| Rok vydání: | 1981 |
| Předmět: |
Hot Temperature
Octoxynol Kinetics Neuraminidase Biochemistry Michaelis–Menten kinetics Polyethylene Glycols chemistry.chemical_compound Drug Stability Freezing Humans Centrifugation Hymecromone Chromatography biology Human liver Hydrogen-Ion Concentration Liver chemistry biology.protein N-Acetylneuraminic acid Homogenization (biology) |
| Zdroj: | International Journal of Biochemistry. 13:975-980 |
| ISSN: | 0020-711X |
| DOI: | 10.1016/0020-711x(81)90002-1 |
| Popis: | 1. 1. The conditions of a linear assay for 4-methylumbelliferyl-α-d-n-acetylneuraminic acid (4-MU-NANA) neuraminidase activity in human liver have been determined and an acidic liver neuraminidase has been characterized with a pH optimum between 4.4 and 4.8 and an apparent Michaelis constant of O.11 ± O.02 mM for 4-MU-NANA. This acidic neuraminidase is labile to freezing, heating and various storage conditions. 2. 2. The great majority of human liver neuraminidase activity is found in resuspended pellets after homogenization and centrifugation. A small amount of this resuspended pellet activity can be solubilized with the nonionic detergent Triton X-100. 3. 3. The properties of human liver neuraminidase are compared to those of other mammalian neuraminidases. |
| Databáze: | OpenAIRE |
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