An intrinsically disordered radish vacuolar calcium-binding protein (RVCaB) showed cryoprotective activity for lactate dehydrogenase with its hydrophobic region.
An intrinsically disordered radish vacuolar calcium-binding protein (RVCaB) showed cryoprotective activity for lactate dehydrogenase with its hydrophobic region.
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本质上无序的萝卜液泡钙结合蛋白（RVCaB）通过其疏水区域显示出对乳酸脱氢酶的冷冻保护活性。
DOI：
10.1016/j.ijbiomac.2021.04.056
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发表时间：
2021
影响因子：
8.2
通讯作者：
Masakazu Hara
中科院分区：
文献类型：
--
作者：
Honami Osuda;Yui Sunano;Masakazu Hara
来自萝卜 (RaphanussativusL.) 主根的可溶性蛋白质组分对乳酸脱氢酶 (LDH) 具有冷冻保护活性。该活性主要存在于可溶性蛋白质的热稳定部分中。经TOYOPEARL SuperQ和TOYOPEARL DEAE连续色谱纯化，十二烷基硫酸钠聚丙烯酰胺凝胶电泳分子量为43 kDa。 MALDI-TOF MS/MS 分析表明纯化的蛋白是萝卜液泡钙结合蛋白 (RVCaB)，据报道该蛋白与萝卜主根液泡中的钙储存有关。纯化的 RVCaB 抑制 LDH 的冷冻失活、冷冻变性和冷冻聚集。 RVCaB 比一般冷冻保护剂具有更强的冷冻保护活性。当RVCaB被分为15个片段（Seg01至Seg15，每个片段15个氨基酸）时，具有高疏水性尺度的Seg03表现出显着的冷冻保护活性。这表明 RVCaB 可能通过特定的疏水区域（即 Seg03）保护 LDH 免受冻融损伤。
A soluble protein fraction from radish (RaphanussativusL.) taproot had cryoprotective activity for lactate dehydrogenase (LDH). The activity was found mainly in the heat-stable fractions of soluble proteins. The cryoprotective protein, whose molecular mass was 43 kDa in sodium dodecyl sulfate polyacrylamide gel electrophoresis, was obtained by successive chromatographies on TOYOPEARL SuperQ and TOYOPEARL DEAE. MALDI-TOF MS/MS analysis indicated that the purified protein was a radish vacuolar calcium-binding protein (RVCaB), which is reportedly related to calcium storage in the vacuoles of radish taproot. The purified RVCaB inhibited the cryoinactivation, cryodenaturation, and cryoaggregation of LDH. RVCaB had greater cryoprotective activity than general cryoprotectants. When RVCaB was divided into 15 segments (Seg01 to Seg15, 15 amino acids each), Seg03, which had a high hydrophobicity scale, showed remarkable cryoprotective activity. This indicated that RVCaB protected LDH from freezing and thawing damage presumably through a specific hydrophobic area (i.e., Seg03).
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