来自大鼠和人肝脏的苯丙氨酸羟化酶刺激蛋白/蝶呤-4α-甲醇胺脱水酶。纯化、特性鉴定及完整氨基酸序列

Phenylalanine hydroxylase-stimulating protein/pterin-4 alpha-carbinolamine dehydratase from rat and human liver. Purification, characterization, and complete amino acid sequence.

作者信息

Hauer C R, Rebrin I, Thöny B, Neuheiser F, Curtius H C, Hunziker P, Blau N, Ghisla S, Heizmann C W

机构信息

Department of Pediatrics, University of Zürich, Switzerland.

出版信息

J Biol Chem. 1993 Mar 5;268(7):4828-31.

PMID:8444860

Abstract

Phenylalanine hydroxylase-stimulating protein, also known as pterin-4 alpha-carbinolamine dehydratase (PHS/PCD), was purified from rat and, for the first time, from human liver. We obtained their complete protein primary sequence using a combination of liquid secondary ionization mass spectrometry/tandem quadrupole mass spectrometry, electrospray ionization mass spectrometry, and Edman microsequence analysis. The amino acid sequences of human and rat PHS/PCD were found to be identical. Surprisingly, the primary structure of PHS/PCD is also essentially identical to a protein of the cell nucleus, named dimerization cofactor of hepatocyte nuclear factor 1 alpha, recently reported to be involved in transcription (Mendel, D. M., Khavari, P. A., Conley, P. B., Graves, M. K., Hansen, L. P., Admon, A., and Crabtree, G. R. (1991) Science 254, 1762-1767).

摘要

苯丙氨酸羟化酶刺激蛋白，也称为蝶呤-4α-甲醇胺脱水酶（PHS/PCD），已从大鼠肝脏中纯化出来，并且首次从人肝脏中纯化出来。我们结合使用液相二次电离质谱/串联四极杆质谱、电喷雾电离质谱和埃德曼微量序列分析获得了它们完整的蛋白质一级序列。发现人和大鼠PHS/PCD的氨基酸序列相同。令人惊讶的是，PHS/PCD的一级结构也与一种细胞核蛋白基本相同，该细胞核蛋白名为肝细胞核因子1α二聚化辅因子，最近报道其参与转录（门德尔，D.M.，哈瓦里，P.A.，康利，P.B.格拉夫斯，M.K.，汉森，L.P.，阿德蒙，A.，和克拉布特里，G.R.（1991年）《科学》254，1762 - 1767）。