01627nas a2200229   4500008004100000022001400041245007400055210006900129260006100198300000900259490000700268520085000275653002101125653001001146653002001156653003101176653001901207100001501226700002501241700002601266856010501292       2008                        eng d  a1572-388700aStudy of papain-cystatin interaction by intensity fading MALDI-TOF-MS0 aStudy of papaincystatin interaction by intensity fading MALDITOF  a233 SPRING STREET, NEW YORK, NY 10013 USAbSPRINGERcJAN  a7-120 v273 a<p>Intensity fading (IF) matrix assisted laser desorption ionization (MALDI) time of flight (TOF) mass spectrometry (MS ) has become an alternative screening approach for the affinity-binding analysis of proteins and peptides with molecular ligands. In this investigation an attempt has been made to study the protein ligand interaction by intensity fading (IF) MALDI-MS using papain and cystatin as model system for protein-ligand interactions. The intensity fading of cystatin was monitored using various concentration of cystatin ranging from (1 to 8.6 mu M) in presence of target protein, papain. The results indeed indicate that the intensity of cystatin decreases upon addition of papain. Furthermore, for the first time we have used IF-MALDI-MS for determining the number of binding sites for cystatin on papain by Scatchard analysis.</p>10aintensity fading10aMALDI10apapain-cystatin10aprotein-ligand interaction10aScatchard plot1 aShabab, M.1 aKulkarni, Mahesh, J.1 aKhan, Mohammad, Islam  uhttps://library.ncl.res.in/content/study-papain-cystatin-interaction-intensity-fading-maldi-tof-ms-0