Rat liver neutral alpha-glucosidase: isolation and characterization.
Neutral alpha-glucosidase was isolated from rat liver by Sephadex G-150 gel filtration and polyacrylamide gel electrophoresis at pH 8.9. The enzyme was found to exist in two major forms: alpha-glucosidase AB and alpha-glucosidase C. The neutral alpha-glucosidase C was purified to apparent homogeneity and biochemically characterized. The enzyme form accounts for 25-30% of the total enzyme activity, has a pH optimum at 6.0-6.5 and is thermostable. The apparent Km values for alpha-glucosidase C with maltose, MUF-alpha-D-glucopyranoside and glycogen as substrates were 1.22 mM, 0.47 mM and 68.9 mg, respectively. The finding that glycogen can serve as substrate for neutral alpha-glucosidase C suggests its involvement in glycogen metabolism.
Lavrenova
T P
TP
Institute of Biomedical Chemistry, Russian Academy of Medical Sciences, Moscow.
Presnova
V N
VN
D000818:Animals; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D004795:Enzyme Stability; D006003:Glycogen / Q000378:metabolism; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D015151:Immunoblotting; D007700:Kinetics; D008099:Liver / Q000201:enzymology*; D051381:Rats; D013379:Substrate Specificity; D013816:Thermodynamics; D000520:alpha-Glucosidases / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism*
D006003:Glycogen; D000520:alpha-Glucosidases