urotensin-i and chloramine

urotensin-i has been researched along with chloramine* in 1 studies

Other Studies

1 other study(ies) available for urotensin-i and chloramine

Article	Year
An oxidation resistant radioligand for corticotropin-releasing factor receptors. Peptides, 2001, Volume: 22, Issue:7 The methionine residues in Tyr-corticotropin-releasing factor (CRF) and Tyr-sauvagine radioligands are subject to oxidation, which renders them biologically inactive. Therefore [Tyr(0,) Gln(1,) Leu(17)]sauvagine (YQLS), in which the methionine was replaced with leucine was synthesized and labeled with (125)Iodine using chloramine-T. Mass spectroscopy revealed that chloramine-T-treatment did not oxidize YQLS. (125)I-YQLS bound with high affinity to cells expressing the murine CRF receptor 1 (CRFR1), CRF receptor 2 (CRFR2), and the mouse brain regions known to express both CRF receptors. (125)I-YQLS chemically cross-linked to CRFR1. In conclusion, (125)I-YQLS is oxidation-resistant, high affinity radioligand that can be chemically cross-linked to the CRF receptors. Topics: Amino Acid Sequence; Amphibian Proteins; Animals; Brain; Cells, Cultured; Chloramines; COS Cells; Cross-Linking Reagents; Cyclic AMP; DNA, Complementary; Dose-Response Relationship, Drug; Iodine; Leucine; Ligands; Mass Spectrometry; Methionine; Mice; Molecular Sequence Data; Oxygen; Peptide Hormones; Peptides; Protein Binding; Receptors, Corticotropin-Releasing Hormone; Sequence Homology, Amino Acid; Succinimides; Tyrosine; Urotensins; Vasodilator Agents	2001

Article

Year

An oxidation resistant radioligand for corticotropin-releasing factor receptors.

Peptides, 2001, Volume: 22, Issue:7

The methionine residues in Tyr-corticotropin-releasing factor (CRF) and Tyr-sauvagine radioligands are subject to oxidation, which renders them biologically inactive. Therefore [Tyr(0,) Gln(1,) Leu(17)]sauvagine (YQLS), in which the methionine was replaced with leucine was synthesized and labeled with (125)Iodine using chloramine-T. Mass spectroscopy revealed that chloramine-T-treatment did not oxidize YQLS. (125)I-YQLS bound with high affinity to cells expressing the murine CRF receptor 1 (CRFR1), CRF receptor 2 (CRFR2), and the mouse brain regions known to express both CRF receptors. (125)I-YQLS chemically cross-linked to CRFR1. In conclusion, (125)I-YQLS is oxidation-resistant, high affinity radioligand that can be chemically cross-linked to the CRF receptors.

Topics: Amino Acid Sequence; Amphibian Proteins; Animals; Brain; Cells, Cultured; Chloramines; COS Cells; Cross-Linking Reagents; Cyclic AMP; DNA, Complementary; Dose-Response Relationship, Drug; Iodine; Leucine; Ligands; Mass Spectrometry; Methionine; Mice; Molecular Sequence Data; Oxygen; Peptide Hormones; Peptides; Protein Binding; Receptors, Corticotropin-Releasing Hormone; Sequence Homology, Amino Acid; Succinimides; Tyrosine; Urotensins; Vasodilator Agents

2001