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The genetic and biochemical properties of the D‐amino acid oxidases in human tissues
Author(s) -
BARKER R. F.,
HOPKINSON D. A.
Publication year - 1977
Publication title -
annals of human genetics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.537
H-Index - 77
eISSN - 1469-1809
pISSN - 0003-4800
DOI - 10.1111/j.1469-1809.1977.tb01959.x
Subject(s) - amino acid , genetics , biology , biochemistry , chemistry , evolutionary biology
SUMMARY 1. Two distinct forms of oxidases catalysing the oxidative deamidation of D‐α‐amino acids have been identified in human tissues: D‐amino acid oxidase (DAMOX) and D‐aspartate oxidase (DASOX). 2. The enzymes differ in their electrophoretic properties, tissue distribution, binding with flavine adenine denucleotide, heat stability, molecular size and possibly in subunit structure. 3. Neither enzyme exhibits genetic polymorphism in European populations, but a rare electrophoretic variant phenotype (DASOX 2‐1) was identified which suggests that the DASOX locus is autosomal and independent of the DAMOX locus.