Hydrodynamic and circular dichroic analysis of mammary-derived growth inhibitor (MDGI).

Abstract

The mammary-derived growth inhibitor exists in solution as a monomeric molecule with a molar mass of 14,500 +/- 400 g/mol. The largest diameter and the height of the polypeptide chain were estimated to be 3.75 +/- 0.25 nm and 2.01 +/- 0.13 nm respectively. This is in good agreement with the structurally related bovine peripheral myelin P2 protein (about 70% amino acid sequence homology). CD measurements have revealed MDGI to be a protein with about 50% beta structure and less than 20% alpha helix similarly as in fatty acid-binding proteins. Removal of endogenous long-chain fatty acid by lipidex or storage in the frozen state lead to a destabilization of the active MDGI conformation which is accompanied by a loss of its activity with regard to growth inhibition of Ehrlich Ascites cells.

• Authors: J Behlke, M Mieth, F D Böhmer, R Grosse
• Journal: Biochemical and biophysical research communications (Biochem Biophys Res Commun) Vol. 161 Issue 1 Pg. 363-70 (May 30 1989) ISSN: 0006-291X [Print] United States
• PMID: 2730664 (Publication Type: Journal Article)

Chemical References

• Carrier Proteins
• FABP3 protein, human
• Fatty Acid Binding Protein 3
• Fatty Acid-Binding Proteins
• Growth Inhibitors
• Peptides
• Solutions

Topics

• Animals
• Carcinoma, Ehrlich Tumor (pathology)
• Carrier Proteins
• Cattle
• Circular Dichroism
• Fatty Acid Binding Protein 3
• Fatty Acid-Binding Proteins
• Growth Inhibitors (pharmacology)
• Humans
• Peptides (pharmacology)
• Protein Conformation
• Solutions
• Spectrum Analysis
• Structure-Activity Relationship
• Swine
• Tumor Cells, Cultured (pathology)