… ’s site I (eg, the warfarin site), whereas Sudlow’s site II … ’s site I, though there are three
secondary sites in domain III, one that accommodates the tyroxine diiodophenol ring in Sudlow’s …

Human serum albumin possesses multiple fatty acid binding sites of varying affinities, but
the precise locations of these sites have remained elusive. The determination of the crystal …

… Ghuman and S. Curry, unpublished observations). For reasons not clear to us, we were unable
… and Curry, S.: Crystal structural analysis of human serum albumin complexed with hemin …

Human serum albumin (HSA) is an abundant plasma protein that binds a remarkably wide
range of drugs, thereby restricting their free, active concentrations. The problem of …

Human serum albumin (HSA) is the most abundant protein in the circulatory system. Its
principal function is to transport fatty acids, but it is also capable of binding a great variety of …

Human serum albumin (HSA) is an abundant transport protein found in plasma that binds a
wide variety of drugs in two primary binding sites (I and II) and can have a significant impact …

Human serum albumin (HSA) is an abundant plasma protein that is responsible for the transport
of fatty acids. HSA also binds and perturbs the pharmacokinetics of a wide range of drug …

Human serum albumin (HSA) is one of the most abundant proteins in the circulatory system
and plays a key role in the transport of fatty acids, metabolites, and drugs. For many drugs, …

Background Human serum albumin (HSA) is an abundant plasma protein that binds a wide
variety of hydrophobic ligands including fatty acids, bilirubin, thyroxine and hemin. Although …

The primary ligands of human serum albumin (HSA), an abundant plasma protein, are non-esterified
fatty acids. In vivo, the majority of fatty acids associated with the protein are …