Binding of uteroglobin to microsomes and plasmatic membranes

FEBS Letters

González, Keybell Díaz¹  Nieto, Antonio¹ 

[1] Centro de Biologia Molecular ‘Severo Ochoa’ (CSIC-UAM), Universidad Autónoma de Madrid, 28049-Cantoblanco, Madrid, Spain

关键词: Membrane protein;    Steroid-binding protein;    Hydrophobic interaction;    Affinity chromatography;   

DOI  :  10.1016/0014-5793(95)00167-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Microsomes and plasmatic membranes from rat liver bind radioactive uteroglobin (UG) in vitro with high affinity (K _d = 1.7 × 10⁻¹⁰ M). The binding is saturable and specific and dependent on previous reduction of UG with dithiothreitol. Microsomes from rat spleen or lung or from rabbit endometrium also possess a similar ability. Binding capacity is not affected by previous treatment of microsomes with phospholipase A₂ or peptide-N-glycosidase F but is lost after brief treatment with trypsin. The complex formed between UG and the binding component can be solubilized from microsomes with 5 mM CHAPS and it elutes with an apparent M _r of 90,000 in a Sephacryl 200 column. The complex is resistant to 8 M urea but is completely dissociated by Triton X-100. The UG-binding protein(s) has been partially purified from solubilized microsomes and membranes by affinity chromatography. The results are discussed in relation to a possible physiological effect of UG on cellular membranes.

【 授权许可】

Unknown