通过氢-氚交换鉴定人血红蛋白中的组氨酸-122α为未知碱性博尔基团之一。
Identification of histidine-122alpha in human haemoglobin as one of the unknown alkaline Bohr groups by hydrogen--tritium exchange.
作者信息
Nishikura K
出版信息
Biochem J. 1978 Aug 1;173(2):651-7. doi: 10.1042/bj1730651.
Abstract
Human carbonmonoxy- and deoxy-haemoglobins were incubated at 37 degrees C in 3H2O at various pH values to measure the pH-dependent hydrogen--tritium exchange at the C-2 position of the imidazole ring of histidine-122alpha. To obtain the pseudo-first-order rate constants for the exchange, k, the two peptides containing histidine-122alpha were isolated and the amounts of tritium incorporated were determined. The rate constants gave pK values for the histidine of 6.1 in carbonmonoxyhaemoglobin and 6.6 in deoxyhaemoglobin, showing that it contributes about 20% to the total alkaline Bohr effect and about 10% at pH7.4.
摘要
将人碳氧血红蛋白和脱氧血红蛋白于37℃在不同pH值的3H2O中孵育，以测量组氨酸-122α咪唑环C-2位上pH依赖性的氢-氚交换。为了获得交换的准一级速率常数k，分离出含组氨酸-122α的两种肽段并测定掺入的氚量。速率常数给出了碳氧血红蛋白中组氨酸的pK值为6.1，脱氧血红蛋白中为6.6，表明它对总碱性玻尔效应的贡献约为20%，在pH7.4时约为10%。
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