[Microcalorimetry study of pharmacological complexes. The binding of cephalosporins with human serum albumin].
Binding of cephazolin, cephalotin and cephamandol to human serum albumin (HSA) was studied by differential scanning calorimetry. It was shown that the binding resulted in an increase in the protein thermostability, while the cooperative character of the biopolymer solution melting was preserved. The constants of association of the above antibiotics with the primary active site of HSA were estimated, with flow microcalorimetry. The complex formation between cephazolin and the protein carrier was mainly due to the ionic forces. Formation of the hydrogen bond was not excluded. The predominating role of hydrophobic interactions in cephalotin and cephamandol binding was shown.
D002152:Calorimetry, Differential Scanning; D002511:Cephalosporins / Q000097:blood*; D006801:Humans; D006863:Hydrogen-Ion Concentration; D066298:In Vitro Techniques; D011485:Protein Binding / Q000187:drug effects; D012709:Serum Albumin / Q000378:metabolism*; D013816:Thermodynamics
D002511:Cephalosporins; D012709:Serum Albumin
Mikrokalorimetricheskoe izuchenie farmakologicheskikh kompleksov. Sviazyvanie s chelovecheskim syvorotochnym al'buminom tsefalosporinov.