Pierce R J, Spik G, Montreuil J
Biochem J. 1980 Jan 1;185(1):261-4. doi: 10.1042/bj1850261.
An endo-N-acetyl-beta-D-glucosaminidase activity towards an asialo-N-acetyl-lactosaminic-type glycoasparagine substrate was demonstrated in rat liver. This activity was optimal at pH 7.0 and was predominantly present in the soluble (cytosolic) fraction.
在大鼠肝脏中证实了一种针对去唾液酸-N-乙酰乳糖胺型糖天冬酰胺底物的内切-N-乙酰-β-D-氨基葡萄糖苷酶活性。该活性在pH 7.0时最佳,主要存在于可溶性(胞质)部分。