A specific hydroxysterol binding protein in human lymphocyte cytosol.
作者： Roselyne E. Defay , Monique E. Astruc , Samia Roussillon , Bernard Descomps , André Crastes de Paulet
DOI: 10.1016/S0300-9084(82)80437-9
关键词: HEPES 、 Chemistry 、 Cell division 、 Biochemistry 、 DNA 、 Thymidine 、 Binding protein 、 HMG-CoA reductase 、 Cytosol 、 Pronase
摘要: A discriminating system capable of recognizing the oxygenated sterols was investigated in human lymphocytes. After labelling entire cells with 25-hydroxy [3H] cholesterol (10 nM) cytosol ultracentrifuged on a linear sucrose density gradient. Bound located single peak sedimentation coefficient 8.3 S. Pronase treatment abolished radioactive peak. This S protein had low binding capacity for and probably high affinity. last parameter not determined account some difficulties encountered cell-free relating to physico-chemical properties 25-hydroxycholesterol. Only hydroxylated closely related 25-hydroxycholesterol were specifically protein, contrast cholesterol. differed from proteins derivatives vitamin D3 glucocorticoids. With lymphocyte as model under our experimental conditions, this sterol-binding seems be involved rather cell division control than regulation HMG-CoA reductase activity: indeed, hydroxysterols able inhibit thymidine incorporation into DNA are recognized by whereas active activity without affecting not.
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