Lavrenova T P, Presnova V N
Institute of Biomedical Chemistry, Russian Academy of Medical Sciences, Moscow.
Biochem Mol Biol Int. 1994 Mar;32(4):671-9.
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.
通过Sephadex G - 150凝胶过滤和pH 8.9条件下的聚丙烯酰胺凝胶电泳从大鼠肝脏中分离出中性α - 葡萄糖苷酶。发现该酶以两种主要形式存在：α - 葡萄糖苷酶AB和α - 葡萄糖苷酶C。中性α - 葡萄糖苷酶C被纯化至表观均一，并进行了生化特性鉴定。该酶形式占总酶活性的25 - 30%，最适pH为6.0 - 6.5，且具有热稳定性。以麦芽糖、MUF - α - D - 吡喃葡萄糖苷和糖原作为底物时，α - 葡萄糖苷酶C的表观Km值分别为1.22 mM、0.47 mM和68.9 mg。糖原可作为中性α - 葡萄糖苷酶C的底物这一发现表明其参与糖原代谢。
