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1 en reported to cyclize to pyroglutamic acid (pGlu) during liquid chromatography (LC)-mass spectrometr
2 he sensitivity and accuracy of Gln, Glu, and pGlu quantitation by electrospray ionization-based mass
3 that we developed to separate Gln, Glu, and pGlu, we found that free Gln and Glu cyclize to pGlu in
7 but cyclization of free Gln and Glu to free pGlu during LC-MS analysis has not been well-characteriz
8 in-G, a 16-amino acid O-linked glycopeptide (pGlu-Ser-Glu-Glu-Gly-Gly-Ser-Asn-Ala-Thr-Lys-Lys-Pro-Tyr
9 he novel (pGlu-Gln)-CCK-8/exendin-4 hybrid, (pGlu-Gln)-CCK-8 alone, or (pGlu-Gln)-CCK-8 in combinatio
10 lian gonadotropin-releasing hormone (GnRH I: pGlu-His-Trp-Ser-Tyr-Gly-Leu-Arg-Pro-Gly-NH2) stimulates
11 of these, designated type II GnRH (GnRH II: pGlu-His-Ser-His-Gly-Trp-Tyr-Pro-Gly-NH2), is conserved
12 actions and therapeutic utility of a novel (pGlu-Gln)-CCK-8/exendin-4 hybrid peptide compared with t
13 Twice-daily administration of the novel (pGlu-Gln)-CCK-8/exendin-4 hybrid, (pGlu-Gln)-CCK-8 alone
15 biguous identification and quantification of pGlu in intact mAbs with natural isotope distribution by
16 d an advantageous system in which removal of pGlu from the heavy chain was determined as a ratio of t
17 3)C and (15)N random coil chemical shifts of pGlu in short reference peptides led to the identificati
19 RIA) revealed that pGlu-Tyr-Pro-NH(2) and/or pGlu-Phe-Pro-NH(2) occur in amygdala, anterior cingulate
20 xendin-4 hybrid, (pGlu-Gln)-CCK-8 alone, or (pGlu-Gln)-CCK-8 in combination with exendin-4 for 21 day
21 , pGlu-His-Pro-NH(2)) and TRH-like peptides (pGlu-X-Pro-NH(2), where "X" can be any amino acid residu
22 thyrotropin-releasing hormone-like peptides (pGlu-X-Pro-NH(2), where "X" can be any amino acid residu
24 procedure for the removal of pyroglutamate (pGlu) by pyroglutamate aminopeptidase (PGAP) and demonst
26 ward protocol, and could detect and quantify pGlu, in agreement with available mass spectrometric dat
27 internal standards to correct for in-source pGlu formation, and (iii) user-optimized fragmentor volt
28 the EEP radioimmunoassay (RIA) revealed that pGlu-Tyr-Pro-NH(2) and/or pGlu-Phe-Pro-NH(2) occur in am
31 ximum of almost 100% of Gln was converted to pGlu in the ionization source, with the extent of conver
32 dration occur not only during cyclization to pGlu, but also during other reactions leading to differe
33 u, we found that free Gln and Glu cyclize to pGlu in the electrospray ionization source, revealing a
34 eleasing hormone (TRH) analogue [Leu(2)]TRH (pGlu-Leu-Pro-NH(2)), was covalently and bioreversibly mo
35 ected and immunoreactivity measured for TRH (pGlu-His-Pro-NH(2)); TRH-Gly, a TRH precursor; Ps4, a pr
36 ted that thyrotropin-releasing hormone (TRH, pGlu-His-Pro-NH(2)) and TRH-like peptides (pGlu-X-Pro-NH