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在无干扰剂的情况下,乳酸脱氢酶在零下温度下的冷诱导变性。

The cold-induced denaturation of lactate dehydrogenase at sub-zero temperatures in the absence of perturbants.

作者信息

Hatley R H, Franks F

机构信息

Pafra Ltd, Biopreservation Division, Cambridge, England.

出版信息

FEBS Lett. 1989 Oct 23;257(1):171-3. doi: 10.1016/0014-5793(89)81813-7.

Abstract

The cold-induced denaturation of lactate dehydrogenase has been determined in an unfrozen, cryoprotectant free solution at sub-zero temperatures. The cold-induced denaturation temperature (TL) has been found to be -28 degrees C. The results for the first time clearly establish that temperature alone can induce denaturation in a cooled protein solution. The validity of earlier data, obtained in the presence of perturbants (particularly pH or guanidinium chloride), is discussed.

摘要

已在零下温度的未冷冻、无冷冻保护剂的溶液中测定了乳酸脱氢酶的冷诱导变性。发现冷诱导变性温度(TL)为-28℃。这些结果首次明确证实,仅温度就能在冷却的蛋白质溶液中诱导变性。文中还讨论了在存在干扰剂(特别是pH值或氯化胍)的情况下获得的早期数据的有效性。

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