Location of the maltosyl isothiocyanate binding site on the human erythrocyte glucose transporter.

Autor: Shelton RL Jr, Langdon RG
Jazyk: angličtina
Zdroj: Biochemistry [Biochemistry] 1985 May 07; Vol. 24 (10), pp. 2397-400.
DOI: 10.1021/bi00331a001
Abstrakt: The covalent affinity probe maltosyl isothiocyanate (MITC) has been used previously to identify the glucose transporter of human erythrocytes as a component of band 3. By use of limited proteolysis, the site on the Mr 100 000 protein to which MITC attaches has been localized to a 17 000-dalton region near the center of the polypeptide chain which is intimately associated with the membrane. The erythrocyte anion transporter, which is probably homologous to the glucose carrier, has a corresponding segment which is known to bind the covalent affinity label 4,4'-diisothiocyano-2,2'-stilbenedisulfonic acid [Ramjeesingh, M., Gaarn, A., & Rothstein, A. (1980) Biochim. Biophys. Acta 559, 127-139]. These results suggest that, in addition to having structural features in common, the two carrier proteins may be quite similar with regard to functional organization.
Databáze: MEDLINE