Salivary peroxidase (SAPX): Genetic modification and relationship to the proline-rich (Pr) and acidic (Pa) proteins

Publisher Website
Google Scholar
Abstract
There is genetic polymorphism of the peroxidase of human saliva, but not of leukocytes. The phenotypes are determined by autosomal inheritance, the phenotype of fast mobility (SAPX 1) being determined by homozygosity for a recessive gene (SAPX 1) and the phenotypes of slow mobility (SAPX 2 and SAPX 3) being determined by two different genes, SAPX 2 and SAPX 3, with completely dominant expression at the same locus. The phenotypes are modified by varying degrees of endogenous proteolysis. The SAPX 2 and SAPX 3 types appear to be genetically controlled modifications of SAPX 1 rather than different primary gene products, because of their completely dominant inheritance, their larger molecular size compared to SAPX 1, and their dissociation with 2-mercaptoethanol to give SAPX 1. The acidic protein type Pa 1 is always found in association with SAPX 2, and an uncommon variant type Pa 2 is associated with SAPX 3. The most likely hypothesis is that the genes Pa 1 and Pa 2 produce products which modify the SAPX 1 type. When the Pa type is Pa 0, the SAPX phenotype is SAPX 1. Since 2-mercaptoethanol can dissociate the Pa 1 protein into a probable monomeric form, and can dissociate SAPX 2 and SAPX 3 to give SAPX 1, it is probable that Pa 1 and Pa 2 monomers complex with SAPX 1 through disulfide bonds to give SAPX 2 or SAPX 3 types. The frequencies of the genes determining the SAPX types are the same as those for Pa: SAPX 1 and Pa 0=0.787, SAPX 2 and Pa 1=0.208, SAPX 3 and Pa 2=0.005.