Apolipoprotein A‐I‐binding protein from human term placenta Purification and partial characterization

FEBS Letters

Lukka, Matti³  Vihko, Pirkko¹  Ehnholm, Christian³  Baumann, Marc²  Olkinuora, Maritta¹  Keso, Leila³ 

[1] Department of Clinical Chemistry, University of Oulu, Oulu, Finland;Recombinant DNA-laboratory, University of Helsinki, Helsinki, Finland;National Public Health Institute, Mannerheimintie 166, Helsinki, Finland

关键词: Apolipoprotein-binding protein;    Apolipoprotein A-I;    Purification;    (Human placenta);   

DOI  :  10.1016/0014-5793(87)80122-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A protein that binds to the main apoprotein, apoA-I, of human high density lipoprotein (HDL) has been isolated from human placenta. Ligand blotting after SDS gel electrophoresis indicated that the 120 kDa protein in the absence of reducing agents binds apoA-I. If gel electrophoresis was performed under reducing conditions two main bands, approx. 50 and 30 kDa that did not bind apoA-I, were evident. In an enzyme-linked immunosorbent assay the binding protein specifically bound apoA-I, delipidated or as HDL. ApoA-II, apo E and LDL did not compete with apoA-I for binding to this protein.

【 授权许可】

Unknown