PRIMARY STRUCTURE AND FUNCTIONAL EXPRESSION OF A GLUTAMINYL CYCLASE

被引:95
作者
POHL, T
ZIMMER, M
MUGELE, K
SPIESS, J
机构
[1] Dept. of Molec. Neuroendocrinology, Max Planck Inst. for Exp. Medicine, 3400 Göttingen
关键词
ENZYME PURIFICATION; PEPTIDE HORMONE BIOSYNTHESIS; POSTTRANSLATIONAL PROCESSING; PROCESSING ENZYME; PYROGLUTAMYL PEPTIDES;
D O I
10.1073/pnas.88.22.10059
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
A glutaminyl cyclase (QC) that is probably involved in the biosynthesis of pyroglutamyl peptides such as gonadotropin-releasing hormone and thyrotropin-releasing hormone has been purified to homogeneity from bovine anterior pituitary. On the basis of N-terminal sequence analysis, a 2088-base-pair cDNA clone was isolated from a bovine anterior pituitary library. From the nucleotide sequence of this clone, the primary structure of a 330-residue protein and a preceding 31-residue prepropeptide sequence was deduced. By transfection of COS-7 monkey cells with a QC cDNA/pCDM8 vector construct, QC activity was expressed. Hybridization with mRNAs of various bovine tissues revealed expression of QC mainly in brain tissue.
引用
收藏
页码:10059 / 10063
页数:5
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