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人T细胞生长因子的翻译后修饰

Posttranslational modification of human T-cell growth factor.

作者信息

Robb R J, Kutny R M, Panico M, Morris H, DeGrado W F, Chowdhry V

出版信息

Biochem Biophys Res Commun. 1983 Nov 15;116(3):1049-55. doi: 10.1016/s0006-291x(83)80248-4.

Abstract

Amino-terminal sequence analysis of human T-cell growth factor indicated that the amino acid in position 3 of the polypeptide chain was modified. Examination of the N-terminal octapeptide using the amino acid analyzer and mass spectrometry demonstrated that position 3 was a threonine which was linked to N-acetyl-D-galactosamine. This site of glycosylation is of practical significance since it appears to play a role in the selectivity of a monoclonal antibody for the factor.

摘要

人T细胞生长因子的氨基末端序列分析表明,多肽链第3位的氨基酸发生了修饰。使用氨基酸分析仪和质谱对N端八肽进行检测,结果显示第3位是与N-乙酰-D-半乳糖胺相连的苏氨酸。这种糖基化位点具有实际意义,因为它似乎在单克隆抗体对该因子的选择性方面发挥作用。

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