Penicillin serum albumin, binding

Penicillins and cephalosporins bind irreversibly to serum albumin. It has been shown that drug-protein conjugates result from the aminolysis of the /3-lactam bond by the e-amino group of lysine residues in the protein (Fig. 5.1, Pathway e). The bound penicilloyl group appears to be the major antigenic determinant of penicillin allergy [145-148],... 

Terasaki, T. Nouda, H. Tsuji, A. Relationship between lipophilicity and binding affinity with human serum albumin for penicillin and cephem antibiotics. J.Pharmacobiodyn., 1992, IS, 99—106... 

Albumin is a protein polypeptide. Albumin has a molecular weight of 66.5 kDa and is the most abundant plasma protein, which is present in the concentration of 35-50 g/L in human serum and is synthesized in the liver. Human serum albumin (HSA) has a half-life of 19 days. It acts as a solubilizing agent for long chain fatty acids and is therefore essential for the transport and metabolism of lipids. It binds very well to penicillins, sulfonamides, indole compounds, benzodiazepines, copper, and nickel in a specific and calcium and zinc in a relatively nonspecific manner. It is responsible for osmotic pressure of the blood. 

Serum albumin is the most abundant plasma protein (3.5-5.5%) and is responsible for the binding and transport of various metabolically and pharmacologically active molecules, e.g., bilirubin, uric acid, vitamin C, acetylcholine, cholinesterase, adenosine, aureomycin, barbiturate, Chloromycetin, digitonin, fatty acids, atabrine, neosilversalvarsan, penicillin, salicylate,/ -aminosalicylate, sulfonamide, streptomycin, acid dyes, histamine, triiodothyronine, and thyroxine (Bennhold, 1962 Putnam, 1975). Moreover, albumin tightly binds various metal ions, e.g., Zn (Giroux,... 

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