甘氨酸导向的肽酰胺化作用：大鼠脑中存在两种将对-谷氨酸-组氨酸-脯氨酸-甘氨酸-OH 转化为对-谷氨酸-组氨酸-脯氨酸-NH2（促甲状腺激素释放激素）的酶。
Glycine-directed peptide amidation: presence in rat brain of two enzymes that convert p-Glu-His-Pro-Gly-OH into p-Glu-His-Pro-NH2 (thyrotropin-releasing hormone).
作者信息
Kizer J S, Busby W H, Cottle C, Youngblood W W
出版信息
Proc Natl Acad Sci U S A. 1984 May;81(10):3228-32. doi: 10.1073/pnas.81.10.3228.
Abstract
To study the possibility of glycine-directed amidation in rat brain, we synthesized the substrate p-Glu-His-Pro-Gly-OH. Adult and neonatal rat brain and adult rat pituitary were sonicated, frozen and thawed, and fractionated by gel permeation chromatography, and fractions from each tissue were assayed for enzymatic activity capable of converting this model substrate into thyrotropin-releasing hormone. We report the presence in rat brain and rat pituitary of two enzymes catalyzing conversion of p-Glu-His-Pro-Gly-OH into thyrotropin-releasing hormone. Based on the differing chemical and physical properties of these two enzymes and their differing affinities for a number of p-Glu-His-Pro-aa-OH analogs (in which aa = glycine, beta-alanine, gamma-butyric acid, and delta-aminovaleric acid), we conclude that there are two distinct enzymatic processes for the terminal amidation of peptides in brain and that COOH-terminal extensions other than glycine are capable of directing COOH-terminal amidation.
摘要
为研究甘氨酸导向的酰胺化反应在大鼠脑中发生的可能性，我们合成了底物对 - 谷氨酸 - 组氨酸 - 脯氨酸 - 甘氨酸 - 羟基（p - Glu - His - Pro - Gly - OH）。将成年和新生大鼠的脑以及成年大鼠的垂体进行超声处理、冷冻和解冻，然后通过凝胶渗透色谱法进行分级分离，并对每个组织的级分检测将该模型底物转化为促甲状腺激素释放激素的酶活性。我们报告在大鼠脑和大鼠垂体中存在两种催化对 - 谷氨酸 - 组氨酸 - 脯氨酸 - 甘氨酸 - 羟基转化为促甲状腺激素释放激素的酶。基于这两种酶不同的化学和物理性质以及它们对多种对 - 谷氨酸 - 组氨酸 - 脯氨酸 - 氨基酸 - 羟基类似物（其中氨基酸 = 甘氨酸、β - 丙氨酸、γ - 丁酸和δ - 氨基戊酸）的不同亲和力，我们得出结论，脑中肽的末端酰胺化存在两种不同的酶促过程，并且除甘氨酸外的羧基末端延伸能够指导羧基末端酰胺化。
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Glycine-directed peptide amidation: presence in rat brain of two enzymes that convert p-Glu-His-Pro-Gly-OH into p-Glu-His-Pro-NH2 (thyrotropin-releasing hormone).甘氨酸导向的肽酰胺化作用：大鼠脑中存在两种将对-谷氨酸-组氨酸-脯氨酸-甘氨酸-OH 转化为对-谷氨酸-组氨酸-脯氨酸-NH2（促甲状腺激素释放激素）的酶。
Proc Natl Acad Sci U S A. 1984 May;81(10):3228-32. doi: 10.1073/pnas.81.10.3228.
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