Abstract
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.
MeSH terms
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Acyltransferases / genetics*
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Acyltransferases / isolation & purification
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Acyltransferases / metabolism
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Amino Acid Sequence
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Aminoacyltransferases*
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Animals
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Base Sequence
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Blotting, Northern
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Cattle
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Cell Line
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Chromatography, High Pressure Liquid
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Chromatography, Ion Exchange
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Cloning, Molecular
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Electrophoresis, Gel, Two-Dimensional
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Gene Library
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Indicators and Reagents
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Kinetics
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Molecular Sequence Data
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Oligonucleotide Probes
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Organ Specificity
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Peptide Fragments / isolation & purification
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Peptides / chemical synthesis
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Pituitary Gland, Anterior / enzymology*
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RNA, Messenger / analysis
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RNA, Messenger / genetics
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RNA, Messenger / isolation & purification
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Transfection
Substances
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Indicators and Reagents
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Oligonucleotide Probes
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Peptide Fragments
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Peptides
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RNA, Messenger
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Acyltransferases
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Aminoacyltransferases
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glutaminyl-peptide cyclotransferase
Associated data
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GENBANK/M80626
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GENBANK/M80632
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GENBANK/S65590
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GENBANK/S65595
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GENBANK/S65600
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GENBANK/X55687
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GENBANK/X55688
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GENBANK/X55689
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GENBANK/X55690
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GENBANK/X56856
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GENBANK/X58180