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- W2054677029 abstract "Isolated cell walls ofMucor rouxii contain substantial amounts of chitin synthetase activity that can be extracted 16 S particles by treatment with digitonin. We developed an efficient procedure to isolate these particles in sufficient quantity and purity to identify their polypeptide components. Growing mycelium ofM.rouxii was labelled with a high radioactive dose of l -[3H]leucine. Cell walls were isolated and packed into a column, and the 16 S chitin synthetase particles extracted with 0.7% digitonin. The 16 S particles were then separated from soluble proteins and lipids by glycerol density gradient centrifugation and purified by consecutive anion and cation exchange HPLC. This purification sequence yielded up to 80 units of chitin synthetase from 10 g dry weight (approximately 60 g wet weight) of mycelium. Specific chitin synthetase activity was as high as 500 nmol GlcNAc min−1 mg protein−1 and was essentially all present as a zymogen. Purified 16 S particles appeared by electron microscopy as a population of isodiametric particles, 80–120A˚in diameter. The 16 S sample became chromatographically homogeneous after a second purification by cation-exchange HPLC: protein and enzyme activity both eluted as a single peak. These 16 S particles are the purest form of chitin synthetase isolated so far fromM. rouxii. SDS-PAGE analysis of all peak fractions revealed up to seven polypeptide bands, four of which (Mr 21, 23, 33, and 39 kDa) were tightly correlated with chitin synthetase activity. The 21-kDa polypeptide was the main component. Since repeated efforts to dissociate 16 S particles into smaller subunits have invariably caused an irreversible loss of chitin synthetase activity, we propose that these four polypeptides form part of a macromolecular complex that synthesizes chitin inM. rouxii." @default.
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- W2054677029 date "1991-03-01" @default.
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- W2054677029 title "Purification and characterization of 16 S chitin synthetase particles from cell walls ofMucor rouxii" @default.
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- W2054677029 doi "https://doi.org/10.1016/0147-5975(91)90003-v" @default.
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