@article{oai:niigata-u.repo.nii.ac.jp:00002527,
 author = {Mikami, Satoshi and Suganuma, Ryo and Hori, Hidetaka and Mitsui, Toshiaki},
 issue = {4},
 journal = {Plant biotechnology},
 month = {Sep},
 note = {Inosine diphosphatase (IDPase) isoforms associated with Golgi membranes were studied in sycamore cell culture. These enzyme isoforms were solubilized with Triton X-100 and purified by chromatography using DEAE-Toyopearl and SOURCE-S columns. The isoforms were separated into two distinguishable fractions (peak 1 and 2) by SOURCE-S column chromatography. Furthermore the peak 1 contained at least two isoform bands detected by native-PAGE analysis. The apparent molecular sizes of these three isoforms were estimated by both gel filtration and SDS-PAGE to be 50 kDa, indicating that the Golgi membrane-bound IDPase has a monomeric structure. These IDPase isoforms required divalent cations (Ca2+, Mg2+, Co2+, Mn2+) for their hydrolyzing activity, and were inhibited by ATP. IDP, UDP, and GDP were effective substrates for these enzymes. It is clearly indicated that the sycamore Golgi membrane-bound IDPase is a nucleoside diphosphatase.},
 pages = {259--265},
 title = {Purification and characterization of golgi membrane-bound nucleoside diphosphatase from suspension-cultured cells of sycamore (acer pseudoplatanus L.)},
 volume = {18},
 year = {2001}
}