A glycophorin is part of a red blood cell. It is technically a sialoglycoprotein which is part of the membrane of the reduction blood cell. The job of a glycophorin protein is mainly to carry sugar molecules. It is around 60% glycosylated. The reason red blood cells can circulate so easily is because of the hydrophilic-charged coat of the protein.
The glycophorin is part of a family of proteins affecting the red blood cells. These are typically named A, B, C, and D based on the quantity of protein present in the membrane. glycophorin A represents the most glycophorin, and glycophorin D represents the least. These proteins can be identified following the separation of the red cell membranes.
There is a fifth glycophorin that has been identified in the human genome, but it is hard to detect during routine gel staining. Overall, glycophorin accounts for around 2% of the total membrane protein mass. You might encounter these glycophorin under other names, too, as they have several discovery members – generally, they're glycophorins.
There are four members in the family of glycophorins. There is A, B, C, and D. The fifth member is hard to detect and therefore often overlooked. The most significant family members are the A and B glycophorins that proliferate in large numbers and variants. The majority of these variants are part of the gene combinations of GYPA and GYPB. Molecular science and medical science need to understand the function and interactions of glycophorins to prevent illnesses and diseases.