PNH and the GPI-Linked Proteins by Neal S. Young (Editor), Joel Moss (Editor)

By Neal S. Young (Editor), Joel Moss (Editor)

Paroxysmal Nocturnal Hemoglobinuria (PNH) has been well-known for over a century. This mysterious ailment is now understood on the point of the gene and the protein. The pathophysiology is said to a category of mobilephone floor proteins with precise biochemical and actual features. lately it's been stated that PNH isn't really infrequent, and as soon as delicate assays--based at the chemistry of the proteins--can be utilized to many patients.Written by means of overseas specialists within the box, this publication contains a variety of particular features, similar to the scientific positive aspects of PNH, the mechanism of hemolysis, the biochemistry of glycosylphosphoinositol anchors, and the chemistry and biophysics of GPI-anchored proteins.This special and well timed quantity may have a large viewers, together with hematologists and oncologists with a scientific curiosity during this disorder, in addition to simple biochemists, immunologists, and cellphone biologists learning this classification of proteins. Key beneficial properties* Outlines the chemical positive factors of PNH* Explains the mechanism of hemolysis* contains paintings at the biochemistry of glycophosphoinositol anchors* includes descriptions of the chemistry and biophysics of GPI-anchored proteins

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A nonfunctional PIG-A pseudogene has been mapped to chromosome 12q21 [9]. The PIG-A Protein The predicted protein product of PIG-A consists of 484 amino acids [5]. A hydrophobic region near the carboxyl terminus may be a transmembrane domain (amino acids 415–442). The hydrophilic carboxyl terminal region of 42 residues corresponds to the luminal domain of PIG-A [14]. There is no amino-terminal hydrophobic signal sequence. A region of 92 amino acids spanning residues 304–395 is homologous (27% identity) to the bacterial glucosaminyl N-acetyl transferase, Rfa K, which is involved in the synthesis of liposaccharides.

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