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151.
Characterization and localization of laccase forms in stem and cell cultures of sycamore 总被引:5,自引:0,他引:5
Azeddine Driouich Anne-Catherine Lainé Brigitte Vian Loic Faye 《The Plant journal : for cell and molecular biology》1992,2(1):13-24
A laccase-type polyphenoloxidase (EC 1.10.3.2.), abundantly secreted by suspension-cultured sycamore (Acer pseudoplatanus) cells was purified to homogeneity. This laccase form is a glycoprotein (molecular weight 110000) with high mannose and complex glycans. The polypeptide moiety has a molecular weight of 66 000, indicating that the glycoprotein is 40% carbohydrate. Laccase is abundantly present in both the cell wall and the culture medium of suspension-cultured sycamore cells, but it is not detected in the cytoplasm, indicating that this large protein is efficiently secreted by the cells. Polyclonal rabbit antiserum was raised against the deglycosylated protein and was used to probe extracts of sycamore stem tissues. A second laccase form (molecular weight 56 000), antigenically related to laccase from cell cultures, is abundant in the epidermis of sycamore stems. In addition, this 56 kDa laccase form co-localizes with lignin precursors on tissue prints from sycamore stems. A polypeptide (molecular weight 50 000-56 000), antigenically related to sycamore laccase, was also immunodetected in most plant organs previously described in the literature as polyphenoloxidase-rich. 相似文献
152.
Azeddine Driouich Pascale Gonnet Mouna Makkie Anne-Catherine Laine Loïc Faye 《Planta》1989,180(1):96-104
Suspension-cultured cells of sycamore (Acer pseudoplatanus L.) secrete a number of acid hydrolases and other proteins that have both highmannose and complex asparagine-linked glycans.
We used affinity chromatography with concanavalin A and an antiserum specific for complex glycans in conjunction with in vivo-labeling
studies to show that all of the secreted proteins carry glycans. The presence of complex glycans on secretory proteins indicates
that they are passing through the Golgi complex on the way to the extracellular compartment. The sodium ionophore, monensin,
did not block the transport of proteins to the extracellular medium, even though monensin efficiently inhibited the Golgi-mediated
processing of complex glycans. The inhibition of N-glycosylation by tunicamycin reduced by 76% to 84% the accumulation of
newly synthesized (i.e. radioactively labeled) protein that was secreted by the sycamore cells, while cytoplasmic protein
biosynthesis was not affected by this antibiotic. However, in the presence of glycoprotein-processing inhibitors, such as
castanospermine and deoxymannojirimycin, the formation of complex glycans was prevented but glycoprotein secretion was unchanged.
These results support the conclusion that N-linked glycan processing is not necessary for sorting, but glycosylation is required
for accumulation of secreted proteins in the extracellular compartment. 相似文献