Michael J. A. Tanner

TL;DR: Results suggest that band 3 forms the core of a macrocomplex of integral and peripheral RBC membrane proteins that may function as an integrated CO(2)/O(2) gas exchange unit (metabolon) in the erythrocyte.

TL;DR: In this paper, the authors found that all affected patients in four families with autosomal dominant familial renal tubular acidosis (dRTA) were heterozygous for mutations in their red cell HCO3/Cl- exchanger, band 3 (AE1, SLC4A1) genes, and these mutations were not found in any of the nine normal family members studied.

TL;DR: The availability of the amino acid sequence allows the interpretation of some of the many studies on the chemical and proteolytic modification of the human protein aimed at examining the structure and mechanism of this membrane transport protein.

TL;DR: Findings underscore the key role of Arg-589 and the C terminus in normal AE1 function, and indicate that while mutations in AE1 cause autosomal dominant dRTA, defects in this gene are not responsible for recessive disease.

TL;DR: The N-terminal 54 amino acid residues of the 30 kDa Rh D polypeptide are determined and sequence data and the polymerase chain reaction (PCR) on human reticulocyte cDNA and genomic DNA are used to clone two types of PCR product of identical size.