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- W1988551451 abstract "An antibody raised against a salt-soluble cell-wall glycoprotein with an apparent molecular weight of 150 kDa cross-reacted with several polypeptide components synthesized by Chlamydomonas reinhardtii wild-type cells and also by the wall-deficient mutant CW- 15. These polypeptides were enriched in LiCI extracts from intact wild-type cells but missing in LiCI extracts from the wall-deficient mutant. The same set of wall-related polypeptides was detected in the culture medium of the mutant CW- 15 but not in the culture medium of wild-type cells. These findings indicate that the wall-deficient mutant CW-15 is able to synthesize the same set of wall-related polypeptides as the wild-type. Immunochemical analyses of in vitro translation products of poly(A)-containing RNA showed that at least four polypeptides with apparent molecular weights of 94 kDa, 67 kDa, 56 kDa and 31 kDa were specifically precipitated by antibodies raised against individual cell-wall glycoproteins with apparent molecular weights of 150 kDa and 35 kDa, respectively. The same wallrelated polypeptides were detected in the in vitro translation products of poly(Aj-containing RNA from wild-type and CW-15 cells. The presence of leader peptide which could be cleaved off by dog pancreatic membranes could be demonstrated only for the 94-kDa component. The pattern of wall-related polypeptides detected in the in vitro translation products of poly(A)-containing RNA corresponded to the pattern of chemically deglycosylated salt-soluble cell-wall glycoproteins. These findings indicate that the cell-wall polypeptides of C. remhardtii are encoded by different mRNA species and that the polypeptide backbones of these cell-wall glycoproteins are structurally related." @default.
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- W1988551451 date "1991-01-01" @default.
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- W1988551451 title "The cell-wall glycoproteins of Chlamydomonas reinhardtii: analysis of the in vitro translation products" @default.
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- W1988551451 doi "https://doi.org/10.1016/0168-9452(91)90017-3" @default.
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