Human leukocyte interferon: a role for disulphide bonds.
Human leukocyte interferon: a role for disulphide bonds.
复制标题
人白细胞干扰素：二硫键的作用。
DOI：
10.1099/0022-1317-22-1-95
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发表时间：
1974
期刊：
影响因子：
--
通讯作者：
K. Cantell
中科院分区：
文献类型：
--
作者：
K. Mogensen;K. Cantell
总结
从部分纯化的白细胞干扰素中回收了一些活性（1 - 10%），该白细胞干扰素已被巯基乙醇还原并在空气中氧化。如果用盐酸胍或尿素解折叠还原的干扰素，则回收完全。在这些变性剂的持续存在下的氧化导致不完全回收（3%）。还原型干扰素的羧甲基化永久性地破坏了所有活性。十二烷基硫酸钠没有引起干扰素活性的任何损失，但在尿素存在下确实阻碍了成功的再氧化。在干扰素结构中至少有一个二硫键的首要重要性。通过二硫键的氧化裂解得到进一步证实。对氯汞苯甲酸盐缺乏效果表明游离巯基对于抗病毒作用并不重要。
Summary
Some activity (1 to 10%) was recovered from partially purified leukocyte interferon which had been reduced by mercaptoethanol and allowed to oxidize in air. The recovery was complete if the reduced interferon was unfolded by guanidine hydrochloride or urea. Oxidation in the continued presence of these denaturants lead to incomplete recovery (3%). Carboxymethylation of reduced interferon permanently destroyed all activity. Sodium dodecyl sulphate did not cause any loss of interferon activity but did hinder successful re-oxidation in the presence of urea. The prime importance of at least one disulphide bond in interferon structure is indicated. Further confirmation was obtained by oxidative cleavage of disulphide bonds. The lack of effect of p-chloro-mercuribenzoate suggests that free thiol groups are not important for antiviral action.