Partial purification of goat kidney beta-mannosidase

1. Goat kidney beta-mannosidase was purified 8500-fold to a specific activity of 65,000 nmol/h per mg of protein with a 6% yield by using multiple steps including cation-exchange and anion-exchange fast protein liquid chromatography. This is the first description of a highly purified preparation fro...

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Bibliographic Details
Published in:Biochemical journal 1988-02, Vol.249 (3), p.871-875
Main Authors: Frei, J.I, Cavanagh, K.T, Fisher, R.A, Hausinger, R.P, Dupuis, M, Rathke, E.J.S, Jones, M.Z
Format: Article
Language:English
Subjects:
Animals
beta -mannosidase
biochemistry
Chromatography, Gel
Chromatography, Ion Exchange
Chromatography, Thin Layer
enzyme activity
Goats
immunology
kidney
Kidney - enzymology
kidneys
Kinetics
Lysosomes - enzymology
mannosidases
Mannosidases - isolation & purification
Mannosidases - metabolism
purification
Substrate Specificity
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Summary:1. Goat kidney beta-mannosidase was purified 8500-fold to a specific activity of 65,000 nmol/h per mg of protein with a 6% yield by using multiple steps including cation-exchange and anion-exchange fast protein liquid chromatography. This is the first description of a highly purified preparation from goat tissue; however, it was not homogeneous, as judged by silver-stained SDS/polyacrylamide-gel electrophoresis. 2. The enzyme exhibited microheterogeneity when analysed by isoelectric focusing (pI 5.5-6.5). 3. Purified beta-mannosidase hydrolysed the terminal beta-(1---4)-linkage of oligosaccharides that accumulate in beta-mannosidosis.
ISSN:0264-6021
1470-8728
DOI:10.1042/bj2490871