title: Biochemical mechanisms of glucose-6-phosphate dehydrogenase deficiency.
abstract: A solid-phase radioimmunoassay for human glucose-6-phosphate dehydrogenase (D-glucose-6-phosphate: NADP+ 1-oxidoreductase; EC 1.1.1.49) was developed that allowed the specific activity of this enzyme protein to be measured in lysates from whole erythrocyte populations, in lysates from erythrocytes of different ages, and in purified samples. The enzyme was highly purified from erythrocytes of single donors by a simple procedure of affinity chromatography with insolubilized adenosine 2',5'-bisphosphate. These techniques were used in an attempt to elucidate the molecular mechanisms leading to deficiency of glucose-6-phosphate dehydrogenase activity in two genetic variants of the enzyme, i.e., the Mediterranean and the Seattle-like variants. The results indicate that the lowered activity of erythrocytes containing the Mediterranean variant of glucose-6-phosphate dehydrogenase is related to an enhanced rate of degradation of a catalytically defective protein synthesized at a nearly normal rate. Synthesis of a normally functioning protein and an increased breakdown of it are involved in the Seattle-like variant of the enzyme.
mesh_terms: D003429:Cross Reactions; D004905:Erythrocyte Aging; D004912:Erythrocytes / Q000201:enzymology; D004913:Erythrocytes, Abnormal / Q000201:enzymology; D005954:Glucosephosphate Dehydrogenase / Q000097:blood* / Q000235:genetics / Q000276:immunology; D005955:Glucosephosphate Dehydrogenase Deficiency / Q000097:blood / Q000201:enzymology* / Q000235:genetics; D006801:Humans; D008297:Male; D010641:Phenotype; D011863:Radioimmunoassay
chemical_list: D005954:Glucosephosphate Dehydrogenase
references.citation: Nature. 1963 Jan 19;197:286-7
references.pmid: 14042175
references.citation: J Clin Invest. 1958 Nov;37(11):1542-8
references.pmid: 13587663
references.citation: J Biol Chem. 1957 Oct;228(2):835-45
references.pmid: 13475364
references.citation: Biochem J. 1953 Oct;55(3):400-8
references.pmid: 13105646
references.citation: J Biol Chem. 1951 Nov;193(1):265-75
references.pmid: 14907713
references.citation: Biochim Biophys Acta. 1977 Nov 7;500(1):109-23
references.pmid: 72567
references.citation: Arch Biochem Biophys. 1977 Mar;179(2):698-705
references.pmid: 15521
references.citation: Br J Haematol. 1974 Oct;28(2):151-5
references.pmid: 4154774
references.citation: Ital J Biochem. 1974 Sep-Oct;23(5):279-91
references.pmid: 4156029
references.citation: J Biol Chem. 1966 Nov 10;241(21):4966-76
references.pmid: 4380840
references.citation: Humangenetik. 1974;25(2):101-9
references.pmid: 4216565
references.citation: Proc Natl Acad Sci U S A. 1972 Apr;69(4):946-50
references.pmid: 4502945
references.citation: J Lab Clin Med. 1974 Jul;84(1):147-51
references.pmid: 4833849
references.citation: Am J Hum Genet. 1969 Mar;21(2):142-53
references.pmid: 5305539
references.citation: Arch Biochem Biophys. 1975 Jul;169(1):362-3
references.pmid: 1155948
references.citation: Clin Chim Acta. 1970 Aug;29(2):209-14
references.pmid: 5493178
references.citation: Eur J Biochem. 1969 Mar;8(1):1-7
references.pmid: 5781268
references.citation: Biochem Biophys Res Commun. 1968 May 10;31(3):501-7
references.pmid: 5653659
references.citation: J Clin Invest. 1968 Apr;47(4):940-8
references.pmid: 5641629
references.citation: J Lab Clin Med. 1967 Apr;69(4):659-74
references.pmid: 6020702
references.citation: Science. 1967 Jan 6;155(3758):97-9
references.pmid: 6015571