The binding of drugs to major human milk whey proteins

Br J Clin Pharmacol. 1988 Jul;26(1):107-9. doi: 10.1111/j.1365-2125.1988.tb03373.x.

Abstract

The binding of nine drugs of diverse physicochemical characteristics to major human milk whey proteins is reported. This group included acids, bases and neutral drugs. No drug bound to alpha-lactalbumin, which is the protein present in greatest concentrations in mature milk. Four drugs, diclofenac, phenytoin, prednisolone and warfarin, bound to albumin but to a much lesser extent than in plasma, consistent with quantitatively less albumin in milk. None of the basic drugs studied bound to albumin. Five drugs, atenolol, diclofenac, prednisolone, propranolol and warfarin, bound to lactoferrin though the extent was minimal except for diclofenac. This group included acids, bases and neutral drugs.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Albumins / metabolism
  • Chemical Phenomena
  • Chemistry
  • Female
  • Humans
  • Lactalbumin / metabolism
  • Lactoferrin / metabolism
  • Milk Proteins / metabolism*
  • Milk, Human / metabolism*
  • Pharmaceutical Preparations / metabolism*
  • Protein Binding
  • Whey Proteins

Substances

  • Albumins
  • Milk Proteins
  • Pharmaceutical Preparations
  • Whey Proteins
  • Lactalbumin
  • Lactoferrin