title: Partial purification of goat kidney beta-mannosidase.
abstract: 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.
authors: Department of Pathology, Michigan State University, East Lansing 48824.
authors: J I
authors: JI
authors: Frei
authors: K T
authors: KT
authors: Cavanagh
authors: R A
authors: RA
authors: Fisher
authors: R P
authors: RP
authors: Hausinger
authors: M
authors: M
authors: Dupuis
authors: E J
authors: EJ
authors: Rathke
authors: M Z
authors: MZ
authors: Jones
mesh_terms: 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
chemical_list: D008361:Mannosidases; D044902:beta-Mannosidase