band 3 protein

These band 3 proteins act as receptors for the parasite.

Between the inner and outer layers of cells is a fatty layer, which band 3 proteins cross many times.

The band 3 protein functions in the transport of chlorine ions and carbonate.

Vitamin E is soluble in fats and is therefore able to enter the region where band 3 proteins reside.

EL4: Southeast Asian ovalocytosis is associated with the Band 3 protein.

SAO is caused by a mutation in the gene encoding the erythrocyte band 3 protein.

Rather, the defect lies in a protein known as the band 3 protein, which lies in the cell membrane itself.

The band 3 protein normally binds to another membrane-bound protein called ankyrin, but in SAO this bond is stronger than normal.

When band 3 proteins deteriorate, for example, when they are repeatedly attacked by the highly reactive form of oxygen known as a free radical, the cell's life is over.

These proteins, known as band 3 proteins, are found in all mammalian cells, which suggests that people and other animals would reap the same benefits as the laboratory mice.

Clustered Band 3 proteins with attached antibodies activate complement, and complement C3 fragments are opsonins recognized by the CR1 complement receptor on phagocytic cells.

There is a deletion of codons 400-408 in the gene, leading to a deletion of 9 amino-acids at the boundary between the cytoplasmic and transmembrane domains of band 3 protein.

These mutations are disease causing as they cause mistargetting of the mutant band 3 proteins so that they are retained within the cell or occasionally addressed to the wrong (i.e. apical) surface.

Hereditary spherocytosis is caused by a variety of molecular defects in the genes that code for spectrin (alpha and beta), ankyrin, band 3 protein, protein 4.2, and other erythrocyte membrane proteins:

The increased rigidity of the erythrocyte membrane in SAO is thought to reduce the capacity of the band 3 proteins to cluster together, thereby making it more difficult for the malaria parasite to properly attaching to and enter the cell.

After much published literature claiming that the ABH substances were all attached to glycosphingolipids, Laine's group (1988) found that the band 3 protein expressed a long polylactosamine chain that contains the major portion of the ABH substances attached.

The Diego Antigen (or Blood Group) System comprises 21 rare blood factors, any of which is carried on the band 3 protein, coded for by the gene SLC4A1 (Solute carrier family 4, Anion exchanger, member 1), located on human chromosome 17.

Band 3 proteins ease the transport of chloride and other negatively charged ions in and out of cells, they are involved in cell respiration and balance of acids and bases and they form the major structural link between the inner and outer "skin" of cells.

Other abnormalities include tighter tethering of the band 3 protein to the cell membrane, increased tyrosine phosphorylation of the band 3 protein, reduced sulfate anion transport through the cell membrane, and more rapid ATP consumption.

The majority of the ABO antigens are expressed on the ends of long polylactosamine chains attached mainly to band 3 protein, the anion exchange protein of the RBC membrane, and a minority of the epitopes are expressed on neutral glycosphingolipid.

Because band 3 proteins weave like an undulating snake through the membranes of cells, they are vulnerable to both free radicals formed inside cells during the course of normal metabolism and to free radicals outside cells that are acquired from the environment and elsewhere in the body and carried in body fluids.

In a report being published today in The Proceedings of the National Academy of Sciences, the Arizona researchers concluded that vitamin E supplements, in amounts equivalent to a human dose of about 400 international units a day, could prolong the life of cells by preventing or delaying oxidative damage to band 3 proteins.