@article{oai:niigata-u.repo.nii.ac.jp:00002520,
 author = {Asakura, Tsuyoshi and Hirose, Shota and Katamine, Hiroki and Kitajima, Aya and Hori, Hidetaka and Sato, Masa and Fujiwara, Masayuki and Shimamoto, Ko and Mitsui, Toshiaki},
 issue = {5},
 journal = {Plant biotechnology},
 month = {Dec},
 note = {The Golgi membranes labeled with cis-Golgi marker GFP-SYP31 were isolated from suspension-cultured cells of rice transformed with 35S::GFP-SYP31 by floating through a discontinuous sucrose density gradient in the presence of 5 mM MgCl2. The specific fluorescence intensity of final membrane preparation increased to approximately 150-fold in comparison with that of the post-nucleus soluble fraction. Specific activity of membrane-bound α-mannosidase (cis-Golgi) markedly increased, but NDPase (medial-/trans-Golgi) and NADPH-cytochrome c reductase endoplasmic reticulum were weakly detected in the membrane fraction. The other organelle marker enzymes, cytochrome c oxidase (mitochondria), alkaline pyrophosphatase (plastid), and catalase (peroxisome) were not detectable. Comparative display of protein spots in GFP-SYP31-labeled membranes, microsomal membranes and soluble fraction on the two dimensional gels showed that some proteins are markedably concentrated in the cis-Golgi membrane fraction. Furthermore, the mass spectrometric analysis of proteins separated by SDS-polyacrylamide gel electrophoresis indicated that the highly purified Golgi membranes contained several membrane traffic-related proteins and ER resident proteins. These findings indicated a close relationship between the ER and the cis-Golgi membranes.},
 pages = {475--485},
 title = {Isolation and proteomic analysis of rice Golgi membranes: cis-Golgi membranes labeled with GFP-SYP31},
 volume = {23},
 year = {2006}
}