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The binding of drugs to major human milk whey proteins.
Author(s) -
Atkinson HC,
Begg EJ
Publication year - 1988
Publication title -
british journal of clinical pharmacology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.216
H-Index - 146
eISSN - 1365-2125
pISSN - 0306-5251
DOI - 10.1111/j.1365-2125.1988.tb03373.x
Subject(s) - warfarin , albumin , chemistry , diclofenac , atenolol , pharmacology , prednisolone , propranolol , drug , plasma protein binding , serum albumin , lactoferrin , blood proteins , phenytoin , biochemistry , medicine , psychiatry , blood pressure , epilepsy , atrial fibrillation
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.