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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
14 d an advantageous system in which removal of pGlu from the heavy chain was determined as a ratio of t
16 RIA) revealed that pGlu-Tyr-Pro-NH(2) and/or pGlu-Phe-Pro-NH(2) occur in amygdala, anterior cingulate
17 xendin-4 hybrid, (pGlu-Gln)-CCK-8 alone, or (pGlu-Gln)-CCK-8 in combination with exendin-4 for 21 day
18 , pGlu-His-Pro-NH(2)) and TRH-like peptides (pGlu-X-Pro-NH(2), where "X" can be any amino acid residu
19 thyrotropin-releasing hormone-like peptides (pGlu-X-Pro-NH(2), where "X" can be any amino acid residu
20 procedure for the removal of pyroglutamate (pGlu) by pyroglutamate aminopeptidase (PGAP) and demonst
21 internal standards to correct for in-source pGlu formation, and (iii) user-optimized fragmentor volt
22 the EEP radioimmunoassay (RIA) revealed that pGlu-Tyr-Pro-NH(2) and/or pGlu-Phe-Pro-NH(2) occur in am
24 ximum of almost 100% of Gln was converted to pGlu in the ionization source, with the extent of conver
25 u, we found that free Gln and Glu cyclize to pGlu in the electrospray ionization source, revealing a
26 eleasing hormone (TRH) analogue [Leu(2)]TRH (pGlu-Leu-Pro-NH(2)), was covalently and bioreversibly mo
27 ected and immunoreactivity measured for TRH (pGlu-His-Pro-NH(2)); TRH-Gly, a TRH precursor; Ps4, a pr
28 ted that thyrotropin-releasing hormone (TRH, pGlu-His-Pro-NH(2)) and TRH-like peptides (pGlu-X-Pro-NH
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