Yvon M, Anglade P, Wal J M
Laboratoire des Sciences de la Consommation, INRA-CRJ, Jouy-en-Josas, France.
FEBS Lett. 1990 Apr 24;263(2):237-40. doi: 10.1016/0014-5793(90)81382-x.
Tryptic digests of fragment A299-585 of penicilloylated serum albumin obtained from two penicillin-treated patients or prepared by in vitro conjugation, were analyzed by a tandem immunoaffinity reversed-phase HLPC. Determinations of benzyl penicilloyl groups (BPO) were performed on the different fractions. Three BPO containing peptides were identified by their amino acid sequence and the bound BPO were located on lysines 432, 541 and 545. Six major BPO binding sites were thus identified on the whole albumin molecule. All of them are lysine residues and correspond to a limited number of definite structures in which lysine and serine residues appear to be closely associated.
从两名接受青霉素治疗的患者身上获取的或通过体外偶联制备的青霉噻唑酰化血清白蛋白片段A299 - 585的胰蛋白酶消化产物,通过串联免疫亲和反相高效液相色谱进行分析。对不同组分进行苄青霉素噻唑基团(BPO)的测定。通过氨基酸序列鉴定出三个含BPO的肽段,且结合的BPO位于赖氨酸432、541和545上。因此在整个白蛋白分子上鉴定出六个主要的BPO结合位点。它们均为赖氨酸残基,且对应于有限数量的特定结构,其中赖氨酸和丝氨酸残基似乎紧密相关。