C-10-O-EQ-N-(4-AZIDO-5-(125)IODO SALICYLOYL)-BETA-ALANYL-BETA ALANYL RYANODINE (AZ-BETA-AR), A NOVEL PHOTO-AFFINITY LIGAND FOR THE RYANODINE BINDING-SITE

Authors
BIDASEE KR BESCH HR KWON S EMMICK JT BESCH KT GERZON K HUMERICKHOUSE RA
Citation
Kr. Bidasee et al., C-10-O-EQ-N-(4-AZIDO-5-(125)IODO SALICYLOYL)-BETA-ALANYL-BETA ALANYL RYANODINE (AZ-BETA-AR), A NOVEL PHOTO-AFFINITY LIGAND FOR THE RYANODINE BINDING-SITE, Journal of labelled compounds & radiopharmaceuticals, 34(1), 1994, pp. 33-47
Citations number
31
Categorie Soggetti
Chemistry Analytical","Pharmacology & Pharmacy
Journal title
Journal of labelled compounds & radiopharmaceuticals → ACNP
ISSN journal
03624803
Volume
34
Issue
1
Year of publication
1994
Pages
33 - 47
Database
ISI
SICI code
0362-4803(1994)34:1<33:CSAR>2.0.ZU;2-2
Abstract
A high affinity, photoactivatable, radio-iodinated ligand for the ryan odine binding site(s) of the sarcoplasmic reticulum calcium-release ch annel, C-10-O(e)-N-(4-azido-5-iodo-125 salicyloyl)-beta-alanyl-beta-al anyl ryanodine (Az-betaAR), was synthesized at a specific activity of 1400mCi/mmol. Prepared by condensing the versatile synthon, N-(4-azido -5-iodo-125 salicyloyl)-beta-alanine with C-10-O(eq)-beta-alanyl ryano dine, Az-betaAR, like [H-3] ryanodine, does not demonstrate saturation binding kinetics. 127Az-betaAR exhibits an IC50 of 27.2 +/- 2 x 10(-9 ) M (mean +/- SD) compared to ryanodine's 6.2 +/- 0.4 x 10(-9) M for t he ryanodine receptor/calcium release channel of sarcoplasmic reticulu m vesicles isolated from rabbit skeletal muscle.