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. 1979 Aug 1;181(2):509–512. doi: 10.1042/bj1810509

Purification and properties of nitrogenase in ethylene glycol at sub-zero temperatures.

A D Tsopanakis, R C Bray, B E Smith
PMCID: PMC1161184  PMID: 387029

Abstract

Both the protein components Kp1 and Kp2 of nitrogenase from Klebsiella pneumoniae were found to be stable in aq. 50% (v/v) ethylene glycol at +30 degrees C or below. At -20 degrees C in this medium their sensitivities to O2 were diminished somewhat. Though purification could be carried out at -20 degrees C, the product had the same specific activity and was obtained in the same yield as when the purification was carried out by standard procedures. This suggests that such procedures yield enzyme undamaged in the course of the purification by O2, thermal denaturation or proteolytic digestion.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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