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- W323202287 abstract "Serial culture of Rhodospirillum rubrum with 2% CO/sub 2/ in H/sub 2/ as the exclusive carbon source resulted in a rather large fraction of the soluble protein (>40%) being comprised of ribulosebisphosphate carboxylase (about sixfold higher than the highest value previously reported). Isolation of the enzyme from these cells revealed that it has physical and kinetic properties similar to those previously described for the enzyme derived from cells grown on butyrate. Notably, the small subunit (which is a constituent of the carboxylase from eucaryotes and most procaryotes) was absent in the enzyme from autotrophically grown R. rubrum. Edman degradation of the purified enzyme revealed that the NH/sub 2/ terminus is free (in contrast to the catalytic subunit of the carboxylase from eucaryotes) and that the NH/sub 2/-terminal sequence is Met-Asp-Gln-Ser-Ser-Arg-Tyr-Val-Asn-Leu-Ala-Leu-Lys-Glu-Glu-Asp-Leu-Ile-Ala-Gly-Gly-Glx-His-Val-Leu-. Crystals of the enzyme were readily obtained by dialysis against distilled water." @default.
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- W323202287 date "1979-01-01" @default.
- W323202287 modified "2023-09-27" @default.
- W323202287 title "Isolation, characterization, and crystallization of ribulosebisphosphate carboxylase from autotrophically grown Rhodospirillum rubrum. [/sup 14/C tracer technique]" @default.
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