Does the fluorescence quencher acrylamide bind to proteins?
We have studied the protein concentration dependence of the acrylamide quenching of the fluorescence of the proteins, human serum albumin and monellin, and we have found no such dependence for the concentration range of 0.5-20 mg/ml. These quenching studies were performed by fluorescence lifetime measurements using phase/modulation fluorometry. We have also performed equilibrium dialysis studies, which show no large degree of association of acrylamide with serum albumin, and we have found that acrylamide has only a small effect on the activity of selected enzymes. These various studies do not indicate the existence of strong acrylamide-protein interactions and are in discord with a recent report by Blatt et al. in this journal (Blatt, E., Husain, A. and Sawyer, W.H. (1986) Biochim. Biophys. Acta 871, 6-13).
Eftink
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Department of Chemistry, University of Mississippi, University 38677.
Ghiron
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CA
D020106:Acrylamide; D000178:Acrylamides / Q000378:metabolism*; D002918:Chymotrypsin / Q000378:metabolism; D003956:Dialysis; D005470:Fluorometry; D007700:Kinetics; D010940:Plant Proteins / Q000378:metabolism; D011485:Protein Binding; D011506:Proteins / Q000378:metabolism*; D012709:Serum Albumin / Q000378:metabolism; D014357:Trypsin / Q000378:metabolism
D000178:Acrylamides; D010940:Plant Proteins; D011506:Proteins; D012709:Serum Albumin; C002541:monellin protein, Dioscoreophyllum cumminsii; D020106:Acrylamide; D002918:Chymotrypsin; D014357:Trypsin