@article{oai:gifu-pu.repo.nii.ac.jp:00006840,
 author = {杉浦, 衛 and 田中, 英郎 and 浅野, 弘 and スギウラ, マモル and タナカ, ヒデオ and アサノ, ヒロシ and Sugiura, Mamoru and Tanaka, Hidero and Asano, Hiroshi},
 journal = {岐阜藥科大學紀要, The annual proceedings of Gifu College of Pharmacy},
 month = {Nov},
 note = {P(論文), The purification and some properties of lipoprotein lipase produced by Pseudomonas sp. were described in this paper. The enzyme was purified about 1100 fold from crude enzyme. The purified enzyme was homogeneity by Tiselius electrophoresis. The optimum pH of this enzyme was about pH 7.3 and with its stability, this enzyme was relatively stable at pH 4.0-7.0. The various bivalent cations had almost no effect on enzyme. As a result of studies on specificity of substrate and various inhibitors, it was demonstrated that microbial lipoprotein lipase was greatly similar to that of the animal tissues except some properties. The activity of animal tissues was inhibited by sodium chloride, protamine sulfate, sodium taurocholate, sodium fluoride, atoxyl and heparin. Whereas, that of the Pseudomonas sp. was not inhibited by atoxyl and heparin.},
 pages = {47--53},
 title = {<原報>酵素剤の研究(29)微生物の産生するLipoprotein Lipaseの研究(その1) : 微生物ならびに動物臓器のLipoprotein Lipaseの酵素的性質(その1)},
 volume = {18},
 year = {1968}
}