Nerli B, Picó G
Departamento de Física-Química, Facultad de Ciencias Bioquímicas and Farmacéuticas (CONICET) (Universidad Nacional de Rosario), Argentina.
Biochem Mol Biol Int. 1994 Mar;32(4):789-95.
The beta lactamase activity of serum albumin was measured using a chromogenic cephalosporin: 3-(2,4 dinitrostyryl) -(6 R, 7R) - 7 -(2 thienacetamido) ceph 3 - em 4 carboxylic acid) (nitrocefin). It was found that albumin of different species and purity, obtained from a variety of sources, showed a significant beta lactamase activity. The reaction presented a saturation kinetics, with a KM of 1.42 10(-5) M. Oleic acid and ibuprofen inhibited the reaction, suggesting that the cephalosporin and these ligands are bound to the same site in albumin. The tertiary structure of albumin is necessary for the catalytic activity to be present probably unprotoned lysine residues in the catalytic site of albumin are related with this activity.
3-(2,4-二硝基苯乙烯基)-(6R,7R)-7-(2-噻吩乙酰胺基)头孢-3-烯-4-羧酸（硝基头孢菌素）来测定血清白蛋白的β-内酰胺酶活性。结果发现，从多种来源获得的不同物种和纯度的白蛋白均表现出显著的β-内酰胺酶活性。该反应呈现出饱和动力学，米氏常数（KM）为1.42×10⁻⁵M。油酸和布洛芬抑制该反应，这表明头孢菌素和这些配体在白蛋白中结合于同一位点。白蛋白的三级结构对于催化活性的存在是必要的，可能白蛋白催化位点中未质子化的赖氨酸残基与该活性有关。
