Partial purification of goat kidney f - mannosidase

1. Goat kidney ,J-mannosidase was purified 8500-fold to a specific activity of 65000 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 (pl 5.5-6.5). 3. Purified ,f-mannosidase hydrolysed the terminal fl-(1-4A)-linkage of oligosaccharides that accumulate in ,l-mannosidosis.