Protein kinase catalysed phosphorylation of monoclonal and polyclonal immunoglobins

F. R. Burnet, C. G. Proud, T. C. Williams

Research output: Contribution to journalArticlepeer-review

Abstract

Radiolabelled tumour directed immunoglobulins have great potential as a means for both locating and treating solid tumours and their metastases. The radiochemical properties of 32P make it a good candidate as a therapeutically useful isotope with which to tag immunoglobulins. We have tested the ability of cyclic AMP dependent protein kinase (cAMP dep PK), Casein Kinase II and Protein Kinase C to phosphorylate both a pan-reactive antiβ tubulin mouse monoclonal (IgG, type 2B, KMX-1) and a selection of polyclonal IgG fractions from different animals. None of the kinases were capable of inserting 32P from [γ-32P]ATP into the native immunoglobulins, but cAMP dep PK was found to be capable of phosphorylating all of the immunoglobulins tested after their partial denaturation in urea. This denaturation was found to be reversible. It was clear from our results that the domain into which 32P is introduced varies markedly between immunoglobulins and we are now extending our studies to discover why this is the case.

Original languageEnglish
Pages (from-to)278-279
Number of pages2
JournalIRCS Medical Science
Volume14
Issue number3
Publication statusPublished - 1986

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

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