大鼠脑α-甘露糖苷酶：纯化、性质及其与抗体的相互作用。

Rat brain alpha-mannosidase: purification, properties, and interaction with its antibodies.

作者信息

Zanetta J P, Meyer A, Dontenwill M, Basset P, Vincendon G

出版信息

J Neurochem. 1982 Dec;39(6):1601-6. doi: 10.1111/j.1471-4159.1982.tb07993.x.

DOI:10.1111/j.1471-4159.1982.tb07993.x

Abstract

Alpha-D-Mannosidase (EC 3.2.1.24.) was purified to homogeneity from adult rat brain. The enzyme, of apparent molecular weight 397,000, appears to be formed of subunits of molecular weight 120,000 made of two protomers (62,000) bound by disulfide bridges. Isoelectric focusing gives two bands, of pI 5.40 and 5.15. Both isoenzymes seem to have the same pH curve (a small peak of activity at pH 4.5 and a maximum of activity around pH 6.0). These two isoenzymes are immunologically related.

摘要

α-D-甘露糖苷酶（EC 3.2.1.24.）从成年大鼠脑中纯化至同质。该酶的表观分子量为397,000，似乎由分子量为120,000的亚基组成，这些亚基由两个原聚体（62,000）通过二硫键结合而成。等电聚焦产生两条带，pI分别为5.40和5.15。两种同工酶似乎具有相同的pH曲线（在pH 4.5处有一个小的活性峰，在pH 6.0左右有最大活性）。这两种同工酶在免疫学上相关。