Characterization of phosphorylation in different phosphorylated forms of insulin-like growth factor-1 receptor (IGF-1R) kinase domain

Luisa Rusconi, Rita Perego, Gianpaolo Fogliatto, M. Beatrice Saccardo, Angela Bachi, Florian Thaler

Research output: Chapter in Book/Report/Conference proceedingConference contribution

Abstract

The in-depth structural characterization of the phospho-isoforms obtained from a construct designed on the basis of sequence homology to the already characterized Insulin Receptor kinase domain (KD) was discussed. Incubation of the construct with ATP yielded a mixture of forms having a phosphorylation level ranging from one to three phosphate moieties per molecule. Six individual forms could be isolated through high-resolution anion-exchange chromatography. Each form was submitted to separate digestion with two enzymes having complementary specificity, namely, trypsin and AspN.

Original languageEnglish
Title of host publicationProceedings - 50th ASMS Conference on Mass Spectrometry and Allied Topics
Pages305-306
Number of pages2
Publication statusPublished - 2002
EventProceedings - 50th ASMS Conference on Mass Spectrometry and Allied Topics - Orlando, FL, United States
Duration: Jun 2 2002Jun 6 2002

Other

OtherProceedings - 50th ASMS Conference on Mass Spectrometry and Allied Topics
CountryUnited States
CityOrlando, FL
Period6/2/026/6/02

ASJC Scopus subject areas

  • Spectroscopy

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    Rusconi, L., Perego, R., Fogliatto, G., Beatrice Saccardo, M., Bachi, A., & Thaler, F. (2002). Characterization of phosphorylation in different phosphorylated forms of insulin-like growth factor-1 receptor (IGF-1R) kinase domain. In Proceedings - 50th ASMS Conference on Mass Spectrometry and Allied Topics (pp. 305-306)