Polypeptide Compositions of Stroma, Internal Membranes, and Inner and Outer Envelope Membranes of Amyloplast from Suspension-Cultured Cells of Sycamore (Acer pseudoplatanus L.)

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Intact amyloplasts isolated from liquid-cultured white-wild cells of sycamore (Acer pseudoplatanus L.) were further subfractionated into internal membranes (d=1.05 g/ml), envelope membranes (d=1.12 g/ml) and stromal fraction, which contained each characteristic polypeptide composition as revealed by the Na-dodecyl sulfate polyacrylamide gel electrophoresis. Absorption spectra of internal and envelope membranes were distinctly different. By the immunoblotting analysis, it was shown that the amyloplast envelope membranes contain 31 kDa P_i-translocator, although it is not the predominant polypeptide component in contrast to the case of chloroplast envelope. One hundred kDa a-1,4-glucan phosphorylase (plastid type) was detected in the stromal fraction of amyloplasts using the specific antibody raised against the major form of a-1,4-glucan phosphorylase from potato tuber. Amyloplast envelopes were further separated into inner and outer membrane fractions by the freezing-thawing method originally developed for the separation of chloroplast envelope membranes by Cline and associates (1981) (Proc. Natl. Acad. Sci. USA 78: 3595-3599). Na-dodecylsulfate gel electrophoretic analysis revealed that the inner and outer envelope membranes contain the distinctly different polypeptide compositions.
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