Arginine residues are involved in the transport function of bilitranslocase
- 1 June 1990
- journal article
- research article
- Published by Elsevier in Biochimica et Biophysica Acta (BBA) - Biomembranes
- Vol. 1025 (2) , 122-126
- https://doi.org/10.1016/0005-2736(90)90088-6
Abstract
No abstract availableKeywords
This publication has 11 references indexed in Scilit:
- The sulfhydryl groups responsible for bilitranslocase transport activity respond to the interaction of the carrier with bilirubin and functional analoguesBiochimica et Biophysica Acta (BBA) - Biomembranes, 1990
- Bilitranslocase is the protein responsible for the electrogenic movement of sulfobromophthalein in plasma membrane vesicles from rat liver: immunochemical evidence using mono- and poly-clonal antibodiesBiochimica et Biophysica Acta (BBA) - Biomembranes, 1989
- The role of sulfhydryl groups in sulfobromophthalein transport in rat liver plasma membrane vesiclesBiochimica et Biophysica Acta (BBA) - Biomembranes, 1989
- The quinoid structure is the molecular requirement for recognition of phthaleins by the organic anion carrier at the sinusoidal plasma membrane level in the liverBiochimica et Biophysica Acta (BBA) - Biomembranes, 1988
- Cellular localization of sulfobromophthalein transport activity in rat liverBiochimica et Biophysica Acta (BBA) - Biomembranes, 1986
- Further studies on bilitranslocase, a plasma membrane protein involved in hepatic organic anion uptakeBiochimica et Biophysica Acta (BBA) - Biomembranes, 1982
- Origin of the Selectivity of α‐Dicarbonyl Reagents for Arginyl Residues of Anion‐Binding SitesEuropean Journal of Biochemistry, 1980
- Isolation of a sulfobromophthalein-binding protein from hepatocyte plasma membraneBiochimica et Biophysica Acta (BBA) - Protein Structure, 1978
- Arginyl Residues: Anion Recognition Sites in EnzymesScience, 1977
- COMBINATION OF THIOL ACIDS WITH METHYLGLYOXALPublished by Elsevier ,1935