Albumin, bovine serum acid transition

Tphe complexing of virtually all purines with aromatic molecules seems - to have far-reaching biological significance. For example, it is known that caffeine affects the rates of many enzymatic reactions (e.g., 0.01, 0.05, and 0.10M caffeine will inhibit salivary amylase 29, 54, and 72% respectively) (12), and purine can decrease the helix-coil transition temperature of the proteins bovine serum albumin and lysozyme (2). It is not unreasonable to expect the involvement of caffeine-aromatic and purine-aromatic complexes because caffeine derivatives and purine complex with the aromatic amino acids tyrosine, phenylalanine, and tryptophan (2). (In fact tryptophan forms a stable 1 to 1 crystalline complex in 0.5M theophylline glycol.)... 

Other protein-rhodium conjugates containing cationic rhodium catalysts have also been prepared using bis(diphenylphosphino-ethyl)amino derivatives 5-7 and solutions of these bis(phosphine) ligands in the presence of carbonic anhydrase, a-chymotrypsin and bovine serum albumin (47). However, the exact nature of the complexes formed has not been discerned in any of these cases, and these latter enzyme-transition metal complexes evidently do not exhibit enantioselectivity in hydrogenation of a-acetamidoacrylic acid. 

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