The Joint Proteomics Research Laboratory, a joint initiative of the Ludwig Institute for Cancer Research and the Walter and Eliza Hall Institute of Medical Research, continues to focus on analytical biochemistry, technical developments in protein separation and characterisation, and Proteomics.
The broad objective of the laboratory is to strive to keep the analytical technology for protein and peptide characterisation at a `cutting-edge' status so that the two Institutes are well positioned to rapidly identify new molecules of biological importance. Undoubtedly, such new technology will help in achieving our goal of providing effective treatments for cancers.

We apply many technical innovations, developed both "in-house" and elsewhere, to:

1. Identify new proteins that are important in cell growth and function,
2. Dissect the intracellular responses to growth factors.

A second laboratory program is to improve our understanding of the structure - function relationships of proteins that are relevant to the cancer process.

• Proteomic identification of serum markers for human colorectal cancer.
• Proteomic analysis of the plasma membrane human colon carcinoma cells.
• Structural determinants of the Human Interleukin-6 Receptor Complex
  
  

Ludwig Institute for Cancer Research to launch Cancer Proteomics Program on 8 March
$1million capital works grant from the Australian Cancer Research Foundation awarded for purchase of mass spectrometer to assist with early detection of colon cancer. The acquisition of a new mass spectrometer configured for direct identification of proteins in complex mixtures will form the technical basis for LICR to establish a dedicated clinical, cancer biomarker capability.

1. Simpson, R.J. and Nice, E.C. (1984) In situ cyanogen bromide cleavage of N-terminally blocked proteins in a gas-phase sequencer. Biochem. Int. 8:787-791.

2. van Driel, I.R., Stearne, P.A., Grego, B., Simpson, R.J. and Goding, J.W. (1984) The receptor for transferrin on murine myeloma cells: One-step purification based on its physiology and partial amino acid sequence. J. Immunol. 133:3220-3224.

3. Stearne, P.A., van Driel, I.R., Grego, B., Simpson, R.J. and Goding, J.W. (1985) The murine plasma cell antigen PC-1: Purification and partial amino acid sequence. J. Immunol. 134:443-448.

4. Grego, B., van Driel, I.R., Stearne, P.A., Goding, J.W., Nice, E.C. and Simpson, R.J. (1985) A microbore high performance liquid chromatography strategy for the purification of polypeptides for gas-phase sequence analysis: Structural studies on the murine transferrin receptor. Eur. J. Biochem. 148:485-491.