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首页> 外文期刊>Journal of bacteriology >Isolation, characterization, and crystallization of ribulosebisphosphate carboxylase from autotrophically grown Rhodospirillum rubrum.
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Isolation, characterization, and crystallization of ribulosebisphosphate carboxylase from autotrophically grown Rhodospirillum rubrum.

机译：自养型红螺螺旋藻的核糖二磷酸羧化酶的分离，鉴定和结晶。

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摘要

Serial culture of Rhodospirillum rubrum with 2% CO2 in H2 as the exclusive carbon source resulted in a rather large fraction of the soluble protein (greater than 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 NH2 terminus is free (in contrast to the catalytic subunit of the carboxylase from eucaryotes) and that the NH2-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.
机译：用2％的H2中的CO2作为唯一碳源的红螺螺旋藻的连续培养导致相当一部分可溶性蛋白（大于40％）由核糖双磷酸羧化酶组成（比先前报道的最高值高约六倍）。从这些细胞中分离出的酶表明，它的物理和动力学性质与先前描述的从丁酸盐上生长的细胞衍生的酶相似。值得注意的是，自养的红景天的酶中没有小亚基（它是真核生物和大多数原核生物的羧化酶的组成部分）。纯化酶的埃德曼降解表明，NH2末端是游离的（与来自真核生物的羧化酶的催化亚基相反），并且NH2末端序列是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-。通过用蒸馏水透析容易获得酶的晶体。

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