A Study of Detergent Pollution By Molecular Methods: Starch Gel Electrophoresis of a Variety of Enzymes and Other Proteins

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Abstract
Tissues from a number of marine species were treated with a variety of solutions, including 1% of the major ‘detergent’ (B.P. 1002) used in attempting to disperse the oil from the ‘Torrey Canyon’ and 1% of each of the three major constituents of B.P. 1002, two of which are non-ionic surfactants.The extracts were submitted to vertical starch-gel electrophoresis in order to measure both the effect of the detergent in facilitating the breakdown of cellular structure (extractability), and the irreversible effect on activation or inhibition of various enzymes and other proteins.The proteins studied include a variety of NAD- and NADP-linked dehydrogenases, esterases, blood and nerve haemoglobins, plasma proteins, egg white and yolk proteins, and r-phycoerythrin.The results confirm the general opinion that detergents increase the extractability of proteins from cells. In particular lipoprotein systems are altered, e.g. ‘fast’ serum lipoprotein in fishes (and other vertebrates). Other effects are also observed, e.g. sole but not turbot haemoglobin is rendered relatively insoluble, probably because the detergent stabilizes haemoglobin binding to other components in the erythrocyte. Certain enzymes, e.g. some esterases and amylases, are activated—a not surprising observation. However, a few enzymes are altered in electrophoretic mobility or in activity in a way that one might not expect, e.g. bass Morone labrax lactate dehydrogenase.The results indicate that ‘oil-spill’ detergents and their constituent surfactants are biochemically quite powerful agents. It is too early to attempt to correlate in vitro and in vivo observations but there is an indication that starch-gel electrophoresis provides a useful supplement to more conventional methods used in the studies on complex pollution problems.