@article{oai:mdu.repo.nii.ac.jp:00001043,
 author = {FUJIMURA, SETSUO and SHIBATA, YUKINAGA and NAKAMURA, TAKESHI},
 issue = {3},
 journal = {松本歯学},
 month = {Dec},
 note = {application/pdf, α-Glucosidase activity was detected in the crude extract of cell and envelope of Capnocytophaga ochracea ATCC 33596. The enzyme associated with the envelope was effectively dissolved by cetyltrimethylammonium bromide. The enzyme was purified from both fractions by combination of ammonium sulfate precipitation, ion-exchage chromatography, gel filtration, and isoelectric focusing. Properties of both enzymes were quite similar: they were basic proteins, metalloenzymes, and most active at pH7.0. They hydrolyzed only p-nitrophenyl-α-D-gluconopyranoside.},
 pages = {285--288},
 title = {α-Glucosidase of Capnocytophaga ochracea; Its Cellular Location, Dissolution, Purification, and Partial Characterization},
 volume = {17},
 year = {1991}
}