Nerli B, García F, Picó G
Departamento de Química-Física, Facultad de Ciencias Bioquímicas y Farmacéuticas and CONICET, Universidad Nacional de Rosario, Argentina.
Biochem Mol Biol Int. 1995 Nov;37(5):909-15.
The interaction of a chromogenic cephalosporin, 3-(2, 4 dinitrostyryl)-(6 R, 7 R) -7(2 thienylacetamido)-ceph 3-em-5-carboxylic acid) (nitrocefin) with human serum albumin was studied. Purified human albumin was showed to have a hydrolase activity, catalyzing the decomposition of the chromogenic cephalosporin. The dimeric and trimeric form of albumin also showed this hydrolase activity. The presence of the following amino acid residues at the catalytic site of albumin was demonstrated: tyrosyls 199 and 411, tryptophan 214, lysyls 195, 225 and 240, histidyl 146, also some argynyls were involucrated.
研究了一种显色头孢菌素，3-(2,4-二硝基苯乙烯基)-(6R,7R)-7-(2-噻吩乙酰胺基)-头孢-3-烯-5-羧酸（硝噻吩青霉烯）与人血清白蛋白的相互作用。纯化的人白蛋白显示具有水解酶活性，催化显色头孢菌素的分解。白蛋白的二聚体和三聚体形式也显示出这种水解酶活性。已证明白蛋白催化位点存在以下氨基酸残基：酪氨酸199和411、色氨酸214、赖氨酸195、225和240、组氨酸146，也涉及一些精氨酸。
