中文摘要：

从沿海的 thermophile Thermus sp 的 thermostable superoxide dismutase (草皮) 。JM1 被部分铵硫酸盐降水， DEAE-Sepharose 层析和 Phenyl-Sepharose 层析的步净化到同质。净化的本国的酶的特定的活动是 1 656 U/mg。从这紧张的草皮基因被克隆并且在 Escherichia coli 的 overexpressed (E。coli ) 。净化的 recombinant 草皮(rSOD ) 的准备酶朊与适当金属盐借助于孵化与 Fe 或 Mn 被重新组成。作为结果，仅仅重新组成 Mn2+ 的 rSOD (Mn-rSOD ) 展出了 1 598 U/mg 的特定的活动。从 Thermus sp 的草皮。JM1 是 Mn 草皮，由 Fe 或 Mn 的特定的活动分析判定重新组成的 rSODs 和到氰化物和 H2O2 的本国的草皮的 insensitivity。本国的草皮和 MnrSOD 决心是有 monomeric 的 homotetramers 26 kDa 和 27.5 kDa 的分子的质量分别地。他们在 50 獡慳 有高 thermostability 吗？

英文摘要：

A thermostable superoxide dismutase （SOD） from the inshore thermophile Thermus sp. JM1 was purified to homogeneity by steps of fractional ammonium sulfate precipitation, DEAE-Sepharose chromatography and Phenyl-Sepharose chromatography. The specific activity of the purified native enzyme was 1 656 U/mg. A sod gene from this strain was cloned and overexpressed in Escherichia coli （E. coli）. The prepared apo-enzyme of the purified recombinant SOD （rSOD） was reconstituted with either Fe or Mn by means of incubation with appropriate metal salts. As a result, only Mn 2＋ - reconstituted rSOD （Mn-rSOD） exhibited the specific activity of 1 598 U/mg. SOD from Thermus sp. JM1 was Mn-SOD, judging by the specific activities analysis of Fe or Mn reconstituted rSODs and the insensitivity of the native SOD to both cyanide and H 2 O 2 . Both the native SOD and Mn- rSOD were determined to be homotetramers with monomeric molecular mass of 26 kDa and 27.5 kDa, respectively. They had high thermostability at 50 ° C and 60 ° C, and showed striking stability across a wide pH span from 4.0 to 11.0.