The site of modification of hemoglobin A by bromotrifluoroacetone?
The site of modification of hemoglobin A by bromotrifluoroacetone?
复制标题
溴三氟丙酮修饰血红蛋白A的位点？
DOI：
10.1016/s0006-291x(75)80350-0
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发表时间：
1975
影响因子：
3.1
通讯作者：
F. Knowles
中科院分区：
文献类型：
--
作者：
F. Knowles
用示踪技术研究了由3-溴-1，1，1-三氟-2-丙酮（BrTFA）生成人血红蛋白三氟丙酮衍生物（HBA-TFA）的过程。在与过量BrTFA反应后，HbA的至少90%的反应性β-93半胱氨酰残基丢失。将HbA-TFA分级分离成血红素、球蛋白、α链和β链并未导致TFA残基预期分离成含有β-93半胱氨酰残基的那些部分。用pCMB在β-93半胱氨酰残基处衍生化的HbA对BrTFA的掺入几乎与未修饰的HbA一样大。HbA和HbA-TFA的半胱氨酸组成，确定为半胱氨酸，没有显着差异。（HbA-pCMB）-TFA的19 F-nmr光谱与HbA-TFA显示的光谱无法区分。这些结果不支持BrTFA与HbA的β-93半胱氨酰残基反应的观点。
The formation of the trifluoracetonyl derivative of human hemoglobin (HBA-TFA) from 3-bromo-1,1,1-trifluoro-2-propanone (BrTFA) has been investigated using tracer techniques. At least 90% of the reactive β-93 cysteinyl residues of HbA were lost following reaction with excess BrTFA. Fractionation of HbA-TFA into heme, globin, α-chains and β-chains did not result in the expected segregation of TFA residues into those moities containing the β-93 cysteinyl residue. The incorporation of BrTFA by HbA which had been derivatized at the β-93 cysteinyl residue with pCMB was nearly as great as with unmodified HbA. The cysteine compositions of HbA and HbA-TFA, determined as cysteic acid, were not significantly different. The 19F-nmr spectrum of (HbA-pCMB)-TFA was indistinguishable from that displayed by HbA-TFA. These results do not support the view that BrTFA reacts with the β-93 cysteinyl residue of HbA.