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 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.
Frei
J I
JI
Department of Pathology, Michigan State University, East Lansing 48824.
Cavanagh
K T
KT
Fisher
R A
RA
Hausinger
R P
RP
Dupuis
M
M
Rathke
E J
EJ
Jones
M Z
MZ
D000818:Animals; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D002855:Chromatography, Thin Layer; D006041:Goats; D007668:Kidney / Q000201:enzymology*; D007700:Kinetics; D008247:Lysosomes / Q000201:enzymology; D008361:Mannosidases / Q000302:isolation & purification* / Q000378:metabolism; D013379:Substrate Specificity; D044902:beta-Mannosidase
D008361:Mannosidases; D044902:beta-Mannosidase