Purification, Crystallization, and Characterization of Neuraminidase from Micromonospora viridifaciens(Biological Chemistry)

概要

論文の詳細を見る
Neuraminidase was purified from the culture filtrate of Micromonospora viridifaciens in 4 steps. After the last step the enzyme appeared to be homogeneous on polyacrylamide gel electrophoresis, and the enzyme was crystallized by the addition of ammonium sulfate. The enzyme did not require Ca^<2+> ions for the activity and was not inhibited by EDTA. The enzyme was active on various sialocompounds such as N-acetylneuraminosyl-lactose (Km = 2.1 mM) and colominic acid (Km = 0.3 mM). The activity was strongly inhibited by a sulfhydryl reagent, p-chloromercuribenzoate, and by oxidizing reagents such as N-bromosuccinimide and iodine. Its catalytic properties were compared with those of various microbial neuraminidases. M. viridifaciens neuraminidase was similar in many respects to Clostridium perfringens enzyme.
社団法人日本農芸化学会の論文
1991-04-23