KINETICS OF FORMATION OF NATIVE RIBONUCLEASE DURING OXIDATION OF REDUCED POLYPEPTIDE CHAIN
KINETICS OF FORMATION OF NATIVE RIBONUCLEASE DURING OXIDATION OF REDUCED POLYPEPTIDE CHAIN
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DOI：
10.1073/pnas.47.9.1309
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发表时间：
1961-01-01
影响因子：
11.1
通讯作者：
WHITE, FH
中科院分区：
文献类型：
--
作者：
ANFINSEN, CB;HABER, E;WHITE, FH
对牛核糖核酸酶的化学和物理研究似乎表明了半胱氨酸残基的正确配对方式，并为氨基酸序列本身存在天然的二级和三级结构提供了证据。对天然蛋白质的旋光和光谱研究表明，在氧化早期形成的一些SS键与天然蛋白质的SS键不同，但经过重排得到天然构型。观察到的最显著的现象是酶活性出现前的显著滞后期，在此期间SH滴度和比旋光度沿一条类似一级反应的曲线变化。在从还原的链形成天然RNase的过程中，SH基团可能通过两种机制中的一种转化为SS键，第一种机制涉及正确的半胱氨酸残基的初始配对，第二种机制涉及随机配对和随后的重新洗牌以产生天然排列。初步认为，在该体系中，SH基团的氧化最初是通过SS键的随机形成发生的，随后在热力学驱动下SS交换的影响下发生重排，最终形成天然RNase。
Chemical and physical studies on bovine RNase seem to indicate the manner of correct pairing of half-cystine residues and to present evidence for the assumption of the native secondary and tertiary structures in the amino acid sequence itself. Optical rotation and spectral studies were also carried out on the native protein which suggest that some of the SS bonds formed during the early stage of oxidation are not identical with those of the native protein but undergo rearrangement to yield the native configuration. The most striking phenomenon observed is the marked lag phase before enzyme activity appears, during which time the SH titer and specific optical rotation change along a curve similar to that of a first order reaction. During the formation of native RNase from the reduced chain, SH groups might be converted to SS bonds by one of two general mechanisms, the first involving the initial pairing of the correct half cystine residues and the second, of random pairing with subsequent reshuffling to yield the native arrangement It is tentatively concluded that oxidation of SH groups in this system occurs initially through random formation of SS bonds with subsequent rearrangement taking place under the influence of SS interchange driven by thermodynamic forces toward the most probable form, native RNase.