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相邻残基对酪氨酸与碘反应活性的影响。

The effect of adjacent residues on the reactivity of tyrosyl with iodine.

作者信息

Takeda Y, Seon B K, Roholt O A, Pressman D

机构信息

Department of Biochemistry Research, Roswell Park Memorial Institute, New York State Department of Health, Buffalo, N.Y. 14203, USA.

出版信息

Biochim Biophys Acta. 1971 Dec 28;251(3):357-62. doi: 10.1016/0005-2795(71)90122-x.

DOI:10.1016/0005-2795(71)90122-x
PMID:11452876
Abstract

The effect of the adjacent amino acid side chain groups on the iodination rate of the tyrosine was studied. The model peptides used were Gly-Tyr-Gly, Leu-Tyr-Leu, Glu-Tyr-Glu, and Lys-Tyr-Lys, in which the tyrosine is sandwiched between two hydrophobic, two negatively charged, or two positively charged residues. The results show only minor differences in the iodination rate of tyrosine in these four peptides. These differences are very small in comparison with those previously observed between the tyrosines of kappa Bence-Jones proteins.

摘要

研究了相邻氨基酸侧链基团对酪氨酸碘化速率的影响。所使用的模型肽为甘氨酸 - 酪氨酸 - 甘氨酸、亮氨酸 - 酪氨酸 - 亮氨酸、谷氨酸 - 酪氨酸 - 谷氨酸和赖氨酸 - 酪氨酸 - 赖氨酸,其中酪氨酸夹在两个疏水、两个带负电荷或两个带正电荷的残基之间。结果表明,这四种肽中酪氨酸的碘化速率仅存在微小差异。与之前在κ本斯 - 琼斯蛋白的酪氨酸之间观察到的差异相比,这些差异非常小。

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