Einhoff W, Rüdiger H
Institut für Pharmazie und Lebensmittelchemie der Universität Würzburg.
Biol Chem Hoppe Seyler. 1988 Mar;369(3):165-9. doi: 10.1515/bchm3.1988.369.1.165.
The alpha-mannosidase from Canavalia ensiformis was characterized with respect to molecular mass, glycoprotein nature, amino-acid composition, enzymic properties and action on animal cells. The enzyme is composed of two pairs of subunits (molecular mass 44 and 66 kDa) which form a tetramer (220 kDa). The larger subunit is glycosylated, the smaller one is not. Both subunits have similar amino-acid compositions. The larger subunit contains a surplus of alanine, aspartic acid/asparagine, histidine, phenylalanine and tyrosine, the smaller one a surplus of glutamic acid/glutamine, serine and threonine. The enzyme is subject to product inhibition by mannose. It stimulates the proliferation of B-lymphocytes from nude mice.
对刀豆中的α-甘露糖苷酶进行了分子量、糖蛋白性质、氨基酸组成、酶学性质以及对动物细胞作用等方面的表征。该酶由两对亚基（分子量分别为44 kDa和66 kDa）组成，形成一个四聚体（220 kDa）。较大的亚基是糖基化的，较小的亚基则不是。两个亚基具有相似的氨基酸组成。较大的亚基含有过量的丙氨酸、天冬氨酸/天冬酰胺、组氨酸、苯丙氨酸和酪氨酸，较小的亚基含有过量的谷氨酸/谷氨酰胺、丝氨酸和苏氨酸。该酶受到甘露糖的产物抑制作用。它能刺激裸鼠B淋巴细胞的增殖。
