Binding of certain substituted phenoxy-acids by bovine serum albumin
Matlib, M.A.; Kirkwood, R.C.; Patterson, J.D.E.
Weed Research 11: 2/3, 190-2
1971
ISSN/ISBN: 0043-1737 DOI: 10.1111/j.1365-3180.1971.tb00995.x
Accession: 014359477
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Summary
The binding of MCPA by bovine serum albumin (BSA) was studied using a gel filtration method in which the appearance of a trough in the elution profile was used as the criterion of binding. The amount of MCPA bound to protein was determined using a range of MCPA concns. while maintaining a constant level of BSA. Absorption was measured in the region where the trough appeared and the area of the trough was plotted against moles of MCPA added. At the pH 7.2 level it was estimated that 5 moles of MCPA/mole of BSA were required to eliminate the trough and this represented the amount of MCPA bound to the protein. The same proportion of binding occurred in identical experiments with 2, 4-D and 2, 4, 5-T but with the corresponding phenoxybutyric acids there was evidence of binding of 7 moles/mole of BSA.