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- W2095351101 abstract "Rat serum albumin and its immediate biosynthetic precursor, proalbumin, were resolved from rat liver smooth microsomes using two dimensional gel electrophoresis. These polypeptides were identified by considering their charge properties (in first dimensional isoelectric focusing), apparent molecular weights (in second dimensional sodium dodecyl sulfate polyacrylamide gel electrophoresis), and in situ radio-iodinated peptide fingerprints in comparisons with pure albumin. Tryptic digestion or alkaline-high salt treatment of microsomes did not affect their content of either polypeptide, while 0.05% deoxycholate completely removed proalbumin and decreased albumin. Lactoperoxidase catalyzed radio-iodination of intact microsomes resulted in significant labelling of proalbumin but virtually no labelling of albumin. These results suggest that a short, internal polypeptide segment of proalbumin is exposed on the outer microsomal surface, whereas the bulk of the protein chain is entrapped by the membrane. It is concluded that some, if not all, of proalbumin in liver smooth endoplasmic reticulum is associated with the membrane which may be important for its subsequent processing." @default.
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- W2095351101 date "1980-05-01" @default.
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- W2095351101 title "Proalbumin is bound to the membrane of rat liver smooth microsomes" @default.
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- W2095351101 doi "https://doi.org/10.1016/s0006-291x(80)80230-0" @default.
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