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- W1978826265 abstract "Apoplastic and vacuolar forms of α-mannosidase from barley leaves were purified (the latter ca 1000-fold). Isoenzymes were separated during purification. They consisted of four subunits with an apparent Mr of 53, 46,40 and 24 × 103 in varying proportions. In two-dimensional electropherograms, the Mr 46 and 40 × 103 polypeptides were separated into two isomeric forms of different isoelectric point. The native proteins focused in a pH gradient at different isoelectric points. Their Mrs ranged between 290 and 270 × 103 as judged from size exclusion chromatography and electrophoretic mobility. The compartmentation of the isoenzymes revealed tissue- and age-specificity." @default.
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- W1978826265 date "1992-02-01" @default.
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- W1978826265 title "Purification and compartmentation of α-mannosidase isoenzymes of barley leaves" @default.
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- W1978826265 doi "https://doi.org/10.1016/0031-9422(92)90012-f" @default.
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