Glutaminyl cyclase (QC) is responsible for the presence of pyroglutamyl residues in many neuroendocrine peptides, An examination of the bovine tissue distribution of QC immunoreactivity, enzyme activity, and mRNA confirmed that QC was abundant in brain and pituitary by all three measures. However, enzymatic activity was considerably more widespread than either immunoreactivity or mRNA, suggesting multiple enzyme forms. Partially purified QC from bovine spleen differed significantly from the known bovine pituitary QC in physical and catalytic properties. We propose that this form of glutaminyl cyclase plays a role in the posttranslational processing of constitutively secreted pGlu-containing proteins, (C) 1999 Federation of European Biochemi...
We have partially sequenced glutaminyl cyclases from several mammalian and one avian species and fou...
AbstractThis paper presents the results obtained when pig anterior pituitary granule lysates are inc...
The formation of a pyroglutamyl residue by enzymatic cyclization of an amino terminus glutamine resi...
Glutaminyl cyclase (QC) is responsible for the presence of pyroglutamyl residues in many neuroendocr...
AbstractGlutaminyl cyclase (QC) is responsible for the presence of pyroglutamyl residues in many neu...
Secretory peptides and proteins are frequently modified by pyroglutamic acid (pE, pGlu) at their N-t...
Glutaminyl cyclase (QC, EC 2.3.2.5) catalyzes the formation of the pyroglutamyl residue present at t...
The mechanism for the post-translational conversion of glutamine to pyroglutamic acid on the N termi...
A cDNA clone for glutaminyl cyclase was isolated from a human pituitary cDNA library and the complet...
Background: Glutaminyl cyclase (QC) forms the pyroglutamyl residue at the amino terminus of numerous...
A cDNA clone for glutaminyl cyclase was isolated from a human pituitary cDNA library and the complet...
AbstractN-terminal pyroglutamate (pGlu) formation from glutaminyl precursors is a posttranslational ...
Current assays for the glutaminyl-peptide cyclizing enzyme, glutaminyl cyclase, have several shortco...
A new TRH-like peptide pyroglutamylglutamylproline-amide (pGlu-Glu-ProNH2) has recently been purifie...
Glutaminyl cyclases (QC) catalyze the formation of neurotoxic pGlu-modified amyloid-β peptides found...
We have partially sequenced glutaminyl cyclases from several mammalian and one avian species and fou...
AbstractThis paper presents the results obtained when pig anterior pituitary granule lysates are inc...
The formation of a pyroglutamyl residue by enzymatic cyclization of an amino terminus glutamine resi...
Glutaminyl cyclase (QC) is responsible for the presence of pyroglutamyl residues in many neuroendocr...
AbstractGlutaminyl cyclase (QC) is responsible for the presence of pyroglutamyl residues in many neu...
Secretory peptides and proteins are frequently modified by pyroglutamic acid (pE, pGlu) at their N-t...
Glutaminyl cyclase (QC, EC 2.3.2.5) catalyzes the formation of the pyroglutamyl residue present at t...
The mechanism for the post-translational conversion of glutamine to pyroglutamic acid on the N termi...
A cDNA clone for glutaminyl cyclase was isolated from a human pituitary cDNA library and the complet...
Background: Glutaminyl cyclase (QC) forms the pyroglutamyl residue at the amino terminus of numerous...
A cDNA clone for glutaminyl cyclase was isolated from a human pituitary cDNA library and the complet...
AbstractN-terminal pyroglutamate (pGlu) formation from glutaminyl precursors is a posttranslational ...
Current assays for the glutaminyl-peptide cyclizing enzyme, glutaminyl cyclase, have several shortco...
A new TRH-like peptide pyroglutamylglutamylproline-amide (pGlu-Glu-ProNH2) has recently been purifie...
Glutaminyl cyclases (QC) catalyze the formation of neurotoxic pGlu-modified amyloid-β peptides found...
We have partially sequenced glutaminyl cyclases from several mammalian and one avian species and fou...
AbstractThis paper presents the results obtained when pig anterior pituitary granule lysates are inc...
The formation of a pyroglutamyl residue by enzymatic cyclization of an amino terminus glutamine resi...