Miller B T
Department of Anatomy & Neurosciences, University of Texas Medical Branch, Galveston 77555-1043, USA.
Biochem Biophys Res Commun. 1996 Jan 5;218(1):377-82. doi: 10.1006/bbrc.1996.0066.
Reaction of the decapeptide gonadotropin releasing hormone (GnRH) with the Bolton-Hunter reagent produced a single major derivative. Mass spectrometric analysis of this derivative at M-Scan Corporation revealed that O-acylation of the Ser4 hydroxyl had occurred. Formation of the O-acylated Ser4 derivative was dependent on the presence of the His2 residue in GnRH. Similar experiments with several unrelated peptides revealed that the Bolton-Hunter reagent will readily acylate hydroxyl groups on serine, tyrosine, and threonine side chains located two positions from a histidine residue (e.g., His-X-Ser). Such O-acylated peptides can be formed under mild reaction conditions and appear to be relatively stable. Recognition of this sequence-specific O-acylation can be critical when labeling peptides with the Bolton-Hunter reagent and when interpreting experiments in which such modified peptides are used.
十肽促性腺激素释放激素（GnRH）与博尔顿-亨特试剂反应产生了一种单一的主要衍生物。在M-Scan公司对该衍生物进行的质谱分析表明，Ser4羟基发生了O-酰化。O-酰化Ser4衍生物的形成取决于GnRH中His2残基的存在。对几种不相关肽进行的类似实验表明，博尔顿-亨特试剂会很容易地酰化位于组氨酸残基两个位置处的丝氨酸、酪氨酸和苏氨酸侧链上的羟基（例如，His-X-Ser）。这种O-酰化肽可以在温和的反应条件下形成，并且似乎相对稳定。在用博尔顿-亨特试剂标记肽以及解释使用此类修饰肽的实验时，识别这种序列特异性O-酰化可能至关重要。
