scholarly journals A new glucose 6-phosphate dehydrogenase(G6PD) variant(G6PD Niigata) with chronic hemolysis and liver hemochromatosis.

1989 ◽  
Vol 78 (1) ◽  
pp. 41-47 ◽  
Author(s):  
Yasuko CHIBA ◽  
Shinichiro TAKIZAWA ◽  
Kenji KISHI ◽  
Akira HATTORI ◽  
Akira SHIBATA ◽  
...  
Keyword(s):  
Chronic Hemolysis ◽  
Glucose 6 Phosphate Dehydrogenase ◽  
G6pd Variant

scholarly journals G-6-PD Long Prairie: a new glucose-6-phosphate dehydrogenase mutant exhibiting normal sensitivity to inhibition by NADPH and accompanied by nonspherocytic hemolytic anemia

Blood ◽  
1977 ◽  
Vol 49 (2) ◽  
pp. 247-251 ◽  
Author(s):  
GJ Johnson ◽  
ME Kaplan ◽  
E Beutler
Keyword(s):  
Enzyme Activity ◽  
Enzymatic Activity ◽  
Alternative Mechanism ◽  
Ph Optimum ◽  
Intracellular Enzyme ◽  
Chronic Hemolysis ◽  
Increased Sensitivity ◽  
Normal Sensitivity ◽  
Glucose 6 Phosphate Dehydrogenase ◽  
Heat Instability

Abstract The enzymatic properties of a new glucose-6-phosphate dehydrogenase (G- 6-PD) variant (G-6-PD Long Prairie) were studied in a white patient with chronic nonspherocytic hemolysis. The red cells were found to have 2.3%-7.7% normal enzymatic activity. The mutant enzyme exhibited marked heat instability, an increased pH optimum, a moderately decreased Km for G-6-P, and increased utilization of 2-deoxyglucose-6-phosphate and deamino NADP. The Km for NADP and Ki for NADPH were both normal. G-6-PD Long Prairie is an interesting new G-6-PD variant that demonstrates that chronic hemolysis can be associated with modestly decreased G-6-PD activity despite normal sensitivity to inhibition by NADPH. Although increased sensitivity to inhibition by NADPH has been postulated to decrease intracellular enzyme activity, resulting in enhanced susceptibility to hemolysis in certain G-6-PD variants with only moderately decreased enzymatic activity, an alternative mechanism of hemolysis, possibly enzyme thermolability, exists in G-6-PD Long Prairie.

Reduced Chronic Hemolysis during High-Dose Vitamin E Administration in Mediterranean-Type Glucose-6-Phosphate Dehydrogenase Deficiency

1980 ◽  
Vol 303 (8) ◽  
pp. 416-420 ◽  
Author(s):  
Laurence Corash ◽  
Stephen Spielberg ◽  
Christos Bartsocas ◽  
Laurence Boxer ◽  
Reuven Steinherz ◽  
...  
Keyword(s):  
Vitamin E ◽  
Dehydrogenase Deficiency ◽  
High Dose ◽  
Chronic Hemolysis ◽  
Glucose 6 Phosphate Dehydrogenase ◽  
High Dose Vitamin

scholarly journals New glucose-6-phosphate dehydrogenase mutations from various ethnic groups

Blood ◽  
1992 ◽  
Vol 80 (1) ◽  
pp. 255-256 ◽  
Author(s):  
E Beutler ◽  
B Westwood ◽  
JT Prchal ◽  
G Vaca ◽  
CS Bartsocas ◽  
...  
Keyword(s):  
Amino Acids ◽  
Ethnic Groups ◽  
Binding Sites ◽  
G6pd Deficiency ◽  
Chronic Hemolysis ◽  
Glucose 6 Phosphate Dehydrogenase ◽  
New Mutations

Seven new mutations that produce glucose 6 phosphate dehydrogenase (G6PD) deficiency are described. Three are in variants that were biochemically characterized and described previously, while four were found in samples that had not been characterized biochemically. Several of the mutations affect the amino acids that are mutated in other G6PD variants. As had been noted previously, variants that are associated with nonspherocytic anemia are located either near the glucose 6 phosphate or the NADP binding sites. Variants more distant from these sites are not associated with chronic hemolysis.

scholarly journals G-6-PD Manchester: A New Variant Associated With Chronic Nonspherocytic Hemolytic Anemia

Blood ◽  
1974 ◽  
Vol 43 (2) ◽  
pp. 271-276 ◽  
Author(s):  
Gillian Milner ◽  
Irvine W. Delamore ◽  
Akira Yoshida
Keyword(s):  
Enzyme Activity ◽  
Substrate Specificity ◽  
Electrophoretic Mobility ◽  
Hemolytic Anemia ◽  
New Variant ◽  
Chronic Hemolysis ◽  
Glucose 6 Phosphate Dehydrogenase

Abstract A variant of glucose-6-phosphate dehydrogenase (G-6-PD) designated G-6-PD Manchester, and associated with chronic nonspherocytic hemolytic anemia, was found in an English male. The electrophoretic mobility at pH 7.0 of this G-6-PD variant is the slowest yet described. Substrate specificity is normal but enzyme activity is markedly inhibited by NADPH, and this is thought to account for the severe chronic hemolysis.

scholarly journals New glucose-6-phosphate dehydrogenase mutations from various ethnic groups

Blood ◽  
1992 ◽  
Vol 80 (1) ◽  
pp. 255-256 ◽  
Author(s):  
E Beutler ◽  
B Westwood ◽  
JT Prchal ◽  
G Vaca ◽  
CS Bartsocas ◽  
...  
Keyword(s):  
Amino Acids ◽  
Ethnic Groups ◽  
Binding Sites ◽  
G6pd Deficiency ◽  
Chronic Hemolysis ◽  
Glucose 6 Phosphate Dehydrogenase ◽  
New Mutations

Abstract Seven new mutations that produce glucose 6 phosphate dehydrogenase (G6PD) deficiency are described. Three are in variants that were biochemically characterized and described previously, while four were found in samples that had not been characterized biochemically. Several of the mutations affect the amino acids that are mutated in other G6PD variants. As had been noted previously, variants that are associated with nonspherocytic anemia are located either near the glucose 6 phosphate or the NADP binding sites. Variants more distant from these sites are not associated with chronic hemolysis.

scholarly journals A Philippino Glucose-6-Phosphate Dehydrogenase Variant (G6PD Union) With Enzyme Deficiency and Altered Substrate Specificity

Blood ◽  
1970 ◽  
Vol 35 (4) ◽  
pp. 506-513 ◽  
Author(s):  
AKIRA YOSHIDA ◽  
ERNST W. BAUR ◽  
ARNO G. MOUTLSKY
Keyword(s):  
Substrate Specificity ◽  
Specific Activity ◽  
Cell Enzyme ◽  
Severe Deficiency ◽  
Genetic Pattern ◽  
Normal Enzyme ◽  
Place Of Origin ◽  
Glucose 6 Phosphate Dehydrogenase ◽  
Variant Enzyme ◽  
G6pd Variant

Abstract A variant of glucose-6-phosphate dehydrogenase (G6PD) associated with altered substrate specificity and severe deficiency of red cell enzyme activity was found in a Philippino male and in his relatives. The genetic pattern was consistent with X-linked inheritance. α-Thalassemia was found in the propositus and in several family members, but there was no interaction between G6PD deficiency and α-thalassemia. This G6PD variant has two pH optima, at pH 5.5 and pH 9.0, while the normal enzyme is inactive at pH 5.5. The substrate specificity of the variant enzyme is different from any known G6PD variant: 2-deoxyglucose-6-phosphate and galactose-6-phosphate are good substrates and deamino-NADP is a better coenzyme than NADP. Although G6PD activity in the variant red cells was only three per cent of normal, quantitative immunologic neutralization suggested that the specific activity of the variant enzyme might be at least ten per cent of that of the normal enzyme. This variant is named after the place of origin, Gd Union.

scholarly journals G6PD Nara: a new class 1 glucose-6-phosphate dehydrogenase variant with an eight amino acid deletion

Blood ◽  
1993 ◽  
Vol 82 (11) ◽  
pp. 3250-3252 ◽  
Author(s):  
A Hirono ◽  
H Fujii ◽  
M Shima ◽  
S Miwa
Keyword(s):  
Amino Acid ◽  
Kinetic Studies ◽  
Nucleotide Sequencing ◽  
Amino Acid Deletion ◽  
New Class ◽  
Class 1 ◽  
Measurable Activity ◽  
Exon 9 ◽  
Glucose 6 Phosphate Dehydrogenase ◽  
G6pd Variant

Abstract In the course of molecular studies on Japanese glucose-6-phosphate dehydrogenase (G6PD) variants using single-strand conformation polymorphisms (SSCP) analysis, we found an unusual class 1 G6PD variant that had nucleotide deletion in exon 9. The patient showed chronic nonspherocytic hemolytic anemia associated with frequent episodes of severe hemolytic attack. The hemolysate exhibited no measurable activity. Although the partially purified enzyme had detectable activity, we could not perform kinetic studies because of its extreme instability. Nucleotide sequencing showed a unique 24 bp deletion at nucleotide 953–976 that predicts an eight amino acid deletion of TKGYLDDP at residue 319–326. While this is one of the most drastic structural alterations found in G6PD variants, the region with the amino acid deletion was distant from both the G6P and NADP+ binding sites and was located in a domain with low sequence homology among species. The comparatively low functional importance of the deleted region may have saved the patient from lethal tissue dysfunction.

scholarly journals G-6-PD Long Prairie: a new glucose-6-phosphate dehydrogenase mutant exhibiting normal sensitivity to inhibition by NADPH and accompanied by nonspherocytic hemolytic anemia

Blood ◽  
1977 ◽  
Vol 49 (2) ◽  
pp. 247-251
Author(s):  
GJ Johnson ◽  
ME Kaplan ◽  
E Beutler
Keyword(s):  
Enzyme Activity ◽  
Enzymatic Activity ◽  
Alternative Mechanism ◽  
Ph Optimum ◽  
Intracellular Enzyme ◽  
Chronic Hemolysis ◽  
Increased Sensitivity ◽  
Normal Sensitivity ◽  
Glucose 6 Phosphate Dehydrogenase ◽  
Heat Instability

The enzymatic properties of a new glucose-6-phosphate dehydrogenase (G- 6-PD) variant (G-6-PD Long Prairie) were studied in a white patient with chronic nonspherocytic hemolysis. The red cells were found to have 2.3%-7.7% normal enzymatic activity. The mutant enzyme exhibited marked heat instability, an increased pH optimum, a moderately decreased Km for G-6-P, and increased utilization of 2-deoxyglucose-6-phosphate and deamino NADP. The Km for NADP and Ki for NADPH were both normal. G-6-PD Long Prairie is an interesting new G-6-PD variant that demonstrates that chronic hemolysis can be associated with modestly decreased G-6-PD activity despite normal sensitivity to inhibition by NADPH. Although increased sensitivity to inhibition by NADPH has been postulated to decrease intracellular enzyme activity, resulting in enhanced susceptibility to hemolysis in certain G-6-PD variants with only moderately decreased enzymatic activity, an alternative mechanism of hemolysis, possibly enzyme thermolability, exists in G-6-PD Long Prairie.

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