Glucose-6-phosphate dehydrogenase deficiency pathophysiology: Difference between revisions

Jump to navigation Jump to search
VisualWikitext
No edit summary
No edit summary
 
(53 intermediate revisions by 3 users not shown)
Line 1: Line 1:
__NOTOC__
__NOTOC__
{{Xyz}}
{{Glucose-6-phosphate dehydrogenase deficiency}}


{{CMG}}; {{AE}} {{MA}}
*{{CMG}}; {{AE}} {{MA}}
==Overview==
==Overview==
The exact pathogenesis of [disease name] is not fully understood.
It is understood that G6PD deficiency is the result of reduced [[Glucose-6-phosphate dehydrogenase]] [[enzyme]] levels. G6PD deficiency is an [[X-linked]] disorder. Glucose-6-phosphate dehydrogenase enzyme oxidizes [[glucose-6-phosphate]] to 6-phosphogluconolactone in pentose phosphate pathway ( [[HMP shunt]]). Glucose-6-phosphate dehydrogenase enzyme also reduces [[nicotinamide adenine dinucleotide phosphate]] ([[NADP]]) to [[NADPH]]. [[NADPH]] is an important cofactor in [[glutathione]] metabolism against [[oxidative]] injury in RBC. In G6PD deficiency, [[oxidative]] stresses can denature [[hemoglobin]] and intravascular [[hemolysis]] in RBC can happen. The gene G6PD is located in the distal long arm of the X chromosome at the Xq28 locus. G6PD B, is the wild type or normal. On microscopic histopathological analysis, Heinz bodies can be visualized as a result of denatured [[hemoglobin]] in peripheral blood smears with supravital staining.
 
==Pathophysiology==
===Physiology===
The normal physiology of G6PD deficiency can be understood as follows:
[[image:G6PD_mechanism.png|550px|left|Mechanism of G6PD]]
<br clear="center" />
 
 
 
 
 


OR


It is thought that [disease name] is the result of / is mediated by / is produced by / is caused by either [hypothesis 1], [hypothesis 2], or [hypothesis 3].


OR


[Pathogen name] is usually transmitted via the [transmission route] route to the human host.


OR


Following transmission/ingestion, the [pathogen] uses the [entry site] to invade the [cell name] cell.


OR




[Disease or malignancy name] arises from [cell name]s, which are [cell type] cells that are normally involved in [function of cells].


OR


The progression to [disease name] usually involves the [molecular pathway].


OR


The pathophysiology of [disease/malignancy] depends on the histological subtype.


==Pathophysiology==
===Physiology===
The normal physiology of [name of process] can be understood as follows:


===Pathogenesis===


Glucose-6-phosphate dehydrogenase (G6PD) deficiency, an X-linked disorder, is the most common enzymatic disorder of red blood cells in humans, affecting more than 400 million people worldwide [1-4]. The clinical expression of G6PD variants encompasses a spectrum of hemolytic syndromes. Affected patients are most often asymptomatic, but many patients have episodic anemia, while a few have chronic hemolysis.


With most G6PD variants, hemolysis is induced in children and adults by the sudden destruction of older, more deficient erythrocytes after exposure to drugs having a high redox potential (including the antimalarial drug primaquine and certain sulfa drugs) or to fava beans, selected infections, or metabolic abnormalities (table 1). However, in the neonate with G6PD deficiency, decreased bilirubin elimination may play an important role in the development of jaundice (see 'Jaundice in neonates' below) [5,6].


Normal enzyme function and the genetics and pathophysiology of G6PD deficiency, including its possible role in protecting against severe malaria, will be reviewed here. The clinical manifestations, diagnosis, and treatment of this disorder are discussed separately. (See "Diagnosis and management of glucose-6-phosphate dehydrogenase (G6PD) deficiency".)


A historical review of the discovery of this defect, its clinical manifestations, detection, population genetics, and molecular biology, written by Dr. Ernest Beutler, a pioneer in the understanding of this disorder, is available [7].


'''FUNCTION OF G6PD''' — Glucose-6-phosphate dehydrogenase catalyzes the initial step in the hexose monophosphate (HMP or pentose phosphate) shunt, oxidizing glucose-6-phosphate to 6-phosphogluconolactone and reducing nicotinamide adenine dinucleotide phosphate (NADP) to NADPH (figure 1). The HMP shunt is the only red cell source of NADPH, a cofactor important in glutathione metabolism.


The main function of the HMP shunt is to protect red blood cells against oxidative injury via the production of NADPH. Red blood cells contain relatively high concentrations of reduced glutathione (GSH), a sulfhydryl-containing tripeptide that functions as an intracellular reducing agent, thereby protecting against oxidant injury. Oxidants, such as superoxide anion (O2-) and hydrogen peroxide, are formed within red cells via reactions of hemoglobin with oxygen and can also be produced by exogenous factors such as drugs and infection. If these oxidants accumulate within red cells, hemoglobin and other proteins are oxidized (see below), leading to loss of function and cell death.


Under normal circumstances, oxidant accumulation does not occur, since these compounds are rapidly inactivated by GSH in conjunction with glutathione peroxidase. These reactions result in the conversion of GSH to oxidized glutathione (GSSG). GSH levels are restored by glutathione reductase which catalyzes the reduction of GSSG to GSH. This reaction requires the NADPH generated by G6PD.


Thus, tight coupling of the HMP shunt to glutathione metabolism is responsible for protecting intracellular proteins from oxidative injury. Almost all hemolytic episodes related to altered HMP shunt and glutathione metabolism are due to G6PD deficiency. Rarely, hemolysis results from deficiencies in GSH synthetic enzymes. (See "Disorders of the hexose monophosphate shunt and glutathione metabolism other than glucose-6-phosphate dehydrogenase deficiency".)
*The exact pathogenesis of [disease name] is not completely understood.
OR
*It is understood that  G6PD deficiency  is the result of reduced Glucose-6-phosphate dehydrogenase enzyme levels. G6PD deficiency is an X-linked disorder.  It is the most common enzymatic disorder of red blood cells. Glucose-6-phosphate dehydrogenase enzyme oxidize glucose-6-phosphate to 6-phosphogluconolactone in pentose phosphate pathway ( HMP shunt).  Glucose-6-phosphate dehydrogenase enzyme also reduces nicotinamide adenine dinucleotide phosphate (NADP) to NADPH. NADPH is an important cofactor in glutathione metabolism against oxidative injury in RBC.Reduced glutathione (GSH) convert to oxidized glutathione (GSSG) by glutathione peroxidase enzyme that prevent oxidant accumulation. Glutathione reductase catalyzes the reduction of GSSG to GSH by NADPH. 
*[Pathogen name] is usually transmitted via the [transmission route] route to the human host.
*Following transmission/ingestion, the [pathogen] uses the [entry site] to invade the [cell name] cell.
*[Disease or malignancy name] arises from [cell name]s, which are [cell type] cells that are normally involved in [function of cells].
*The progression to [disease name] usually involves the [molecular pathway].
*The pathophysiology of [disease/malignancy] depends on the histological subtype.


Glucose-6-phosphate dehydrogenase (G6PD) is an enzyme in the pentose phosphate pathway (see image, also known as the HMP shunt pathway). G6PD converts glucose-6-phosphate into 6-phosphoglucono-δ-lactone and is the rate-limiting enzyme of this metabolic pathway that supplies reducing energy to cells by maintaining the level of the reduced form of the co-enzyme nicotinamide adenine dinucleotide phosphate (NADPH). The NADPH in turn maintains the supply of reduced glutathione in the cells that is used to mop up free radicals that cause oxidative damage.


The G6PD / NADPH pathway is the ''only'' source of reduced glutathione in red blood cells (erythrocytes). The role of red cells as oxygen carriers puts them at substantial risk of damage from oxidizing free radicals except for the protective effect of G6PD/NADPH/glutathione.


People with G6PD deficiency are therefore at risk of hemolytic anemia in states of oxidative stress. Oxidative stress can result from infection and from chemical exposure to medication and certain foods. Broad beans, e.g., fava beans, contain high levels of vicine, divicine, convicine and isouramil, all of which create oxidants.


When all remaining reduced glutathione is consumed, enzymes and other proteins (including hemoglobin) are subsequently damaged by the oxidants, leading to cross-bonding and protein deposition in the red cell membranes. Damaged red cells are phagocytosed and sequestered (taken out of circulation) in the spleen. The hemoglobin is metabolized to bilirubin (causing jaundice at high concentrations). The red cells rarely disintegrate in the circulation, so hemoglobin is rarely excreted directly by the kidney, but this can occur in severe cases, causing acute renal failure.


Deficiency of G6PD in the alternative pathway causes the buildup of glucose and thus there is an increase of advanced glycation endproducts (AGE). The deficiency also reduces the amount of NADPH, which is required for the formation of nitric oxide (NO). The high prevalence of diabetes mellitus type 2 and hypertension in Afro-Caribbeans in the West could be directly related to the incidence of G6PD deficiency in those populations.


Although female carriers can have a mild form of G6PD deficiency (dependent on the degree of inactivation of the unaffected X chromosome – see ''lyonization''), homozygous females have been described; in these females there is co-incidence of a rare immune disorder termed chronic granulomatous disease (CGD).
===Pathogenesis===
*It is understood that G6PD deficiency is the result of reduced [[Glucose-6-phosphate dehydrogenase]] [[enzyme]] levels. G6PD deficiency is an [[X-linked]] disorder.  It is the most common enzymatic disorder of [[Red blood cell|red blood cells]]. Glucose-6-phosphate dehydrogenase enzyme oxidizes [[glucose-6-phosphate]] to 6-phosphogluconolactone in pentose phosphate pathway ( [[HMP shunt]]). Glucose-6-phosphate dehydrogenase enzyme also reduces [[nicotinamide adenine dinucleotide phosphate]] ([[NADP]]) to [[NADPH]]. [[NADPH]] is an important cofactor in [[glutathione]] metabolism against [[oxidative]] injury in RBC. Reduced glutathione (GSH) convert to oxidized glutathione (GSSG) by glutathione peroxidase enzyme that prevents [[oxidant]] accumulation. [[Glutathione reductase]] catalyzes the reduction of GSSG to GSH by NADPH. In G6PD deficiency, [[oxidative]] stresses can denature [[hemoglobin]] and intravascular [[hemolysis]] in RBC can happen. [[Infection]], some medications and foods with high level of convicine, vicine, divicine and isouramil such as fava beans can cause oxidative stress. The [[spleen]] is the organ for sequestration damaged RBC. The [[hemoglobin]] is metabolized to [[bilirubin]] and cause [[jaundice]].  


==Genetics==
==Genetics==
[Disease name] is transmitted in [mode of genetic transmission] pattern.
G6PD deficiency is transmitted in [[x-linked]] disorder pattern. The gene G6PD is located in the distal long arm of the X chromosome at the Xq28 locus. <ref name="pmid14033020">{{cite journal |vauthors=KIRKMAN HN, HENDRICKSON EM |title=Sex-linked electrophoretic difference in glucose-6-phosphate dehydrogenase |journal=Am. J. Hum. Genet. |volume=15 |issue= |pages=241–58 |date=September 1963 |pmid=14033020 |pmc=1932381 |doi= |url=}}</ref>


OR
[[Heterozygous]] women are usually normal because of [[lyonization]] ( X innactivation)<ref name="pmid13868717">{{cite journal |vauthors=BEUTLER E, YEH M, FAIRBANKS VF |title=The normal human female as a mosaic of X-chromosome activity: studies using the gene for C-6-PD-deficiency as a marker |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=48 |issue= |pages=9–16 |date=January 1962 |pmid=13868717 |pmc=285481 |doi= |url=}}</ref>


Genes involved in the pathogenesis of [disease name] include:
G6PD B, is the wild type or normal. G6PD has 400 variant [[enzymes]]. <ref name="pmid7949118">{{cite journal |vauthors=Beutler E |title=G6PD deficiency |journal=Blood |volume=84 |issue=11 |pages=3613–36 |date=December 1994 |pmid=7949118 |doi= |url=}}</ref> Caucasians, Asians and majority of blacks has G6PD B. 
*[Gene1]
*[Gene2]
*[Gene3]


OR
G6PD A+: In Africa, in 20-30 percent of black. In this variant, asparagine is substitued for aspartate, at amino acid 126. <ref name="pmid16591538" /> It has normal enzyme activity.


The development of [disease name] is the result of multiple genetic mutations such as:
The development of G6PD deficency is the result of [[Missense mutation|missense]] point mutations and also a few deletions. <ref name="pmid2190319">{{cite journal |vauthors=Beutler E |title=The genetics of glucose-6-phosphate dehydrogenase deficiency |journal=Semin. Hematol. |volume=27 |issue=2 |pages=137–64 |date=April 1990 |pmid=2190319 |doi= |url=}}</ref>
 
*[Mutation 1]
*[Mutation 2]
*[Mutation 3]


*G6PD A+:In Africa, in 20-30 percent of black. In this variant, [[asparagine]] is substitued for [[aspartate]], at [[amino acid]] 126. <ref name="pmid16591538">{{cite journal |vauthors=Yoshida A |title=A single amino Acid substitution (asparagine to aspartic Acid) between normal (b+) and the common negro variant (a+) of human glucose-6-phosphate dehydrogenase |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=57 |issue=3 |pages=835–40 |date=March 1967 |pmid=16591538 |pmc=335583 |doi= |url=}}</ref> It has normal enzyme activity.
*G6PD A-: Cause [[primaquine]] sensitivity in blacks. 
*G6PD mediterranean variant: Single base substitution (C—>T) at nucleotide 563 <ref name="pmid3393536">{{cite journal |vauthors=Vulliamy TJ, D'Urso M, Battistuzzi G, Estrada M, Foulkes NS, Martini G, Calabro V, Poggi V, Giordano R, Town M |title=Diverse point mutations in the human glucose-6-phosphate dehydrogenase gene cause enzyme deficiency and mild or severe hemolytic anemia |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=85 |issue=14 |pages=5171–5 |date=July 1988 |pmid=3393536 |pmc=281710 |doi= |url=}}</ref> 
*
*       
*
*
*G6PD variants in Asia:
**In China: G6PD Canton (1376 G—>T), G6PD Kaiping (1388 G—>A), G6PD Gaohe (95 G—>A)<ref name="pmid4379606">{{cite journal |vauthors=McCurdy PR, Kirkman HN, Naiman JL, Jim RT, Pickard BM |title=A Chinese variant of glucose-6-phosphate dehydrogenase |journal=J. Lab. Clin. Med. |volume=67 |issue=3 |pages=374–85 |date=March 1966 |pmid=4379606 |doi= |url=}}</ref>
**In Southeast Asia: G6PD Mahidol (487G—>A)
**
==Associated Conditions==
==Associated Conditions==
 
* G6PD A− and G6PD Mediterranean has protective effect against ''[[Plasmodium falciparum]]'' and ''[[Plasmodium vivax]]'' malaria. <ref name="pmid2669996">{{cite journal |vauthors=Nagel RL, Roth EF |title=Malaria and red cell genetic defects |journal=Blood |volume=74 |issue=4 |pages=1213–21 |date=September 1989 |pmid=2669996 |doi= |url=}}</ref>
* G6PD deficency is a risk factor of male neonatal sepsis<ref name="pmid27974910">{{cite journal |vauthors=Rostami-Far Z, Ghadiri K, Rostami-Far M, Shaveisi-Zadeh F, Amiri A, Rahimian Zarif B |title=Glucose-6-phosphate dehydrogenase deficiency (G6PD) as a risk factor of male neonatal sepsis |journal=J Med Life |volume=9 |issue=1 |pages=34–38 |date=2016 |pmid=27974910 |pmc=5152609 |doi= |url=}}</ref>
*
==Gross Pathology==
==Gross Pathology==
On gross pathology, [feature1], [feature2], and [feature3] are characteristic findings of [disease name].
On gross pathology,there are no characteristic findings of G6PD deficiency.  


==Microscopic Pathology==
==Microscopic Pathology==
On microscopic histopathological analysis, [feature1], [feature2], and [feature3] are characteristic findings of [disease name].
On microscopic histopathological analysis, Heinz bodies can be visualized as a result of denatured [[hemoglobin]] in peripheral blood smears with supravital staining. (Heinz body prep).<ref name="pmid5425759">{{cite journal |vauthors=Jacob HS |title=Mechanisms of Heinz body formation and attachment to red cell membrane |journal=Semin. Hematol. |volume=7 |issue=3 |pages=341–54 |date=July 1970 |pmid=5425759 |doi= |url=}}</ref>
 
{| align="right"
|
 
[[File:Heinz bodies.jpg|300px|thumb|Heinz bodies , via wikipedia.org<ref>From en.wikipedia.org, Public Domain, <"https://commons.wikimedia.org/w/index.php?curid=">4647353</ref>]]
 
|}
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 


==References==
{{Reflist|2}}


{{WH}}
{{WS}}
[[Category: (name of the system)]]
{{Glucose-6-phosphate dehydrogenase deficiency}}
{{CMG}}; '''Associate Editor(s)-In-Chief:''' [[Priyamvada Singh|Priyamvada Singh, M.D.]] [mailto:psingh13579@gmail.com]


Please help WikiDoc by adding content here.  It's easy!  Click  [[Help:How to Edit a Page|here]]  to learn about editing.


==Overview==


==Pathophysiology==


*


[[image:G6PD_mechanism.png|550px|left|Mechanism of G6PD]]
<br clear="center" />


==References==
==References==
{{reflist|2}}
{{Reflist|2}}


{{WikiDoc Help Menu}}
{{WH}}
{{WikiDoc Sources}}
{{WS}}
 
[[Category: (name of the system)]]
[[Category:Disease]]
[[Category:Hematology]]
[[Category:Mature chapter]]
[[Need content]]

Latest revision as of 15:49, 25 October 2018

Glucose-6-phosphate dehydrogenase deficiency Microchapters

Home

Patient Information

Overview

Historical Perspective

Classification

Pathophysiology

Causes

Differentiating Glucose-6-phosphate dehydrogenase deficiency from other Diseases

Epidemiology and Demographics

Risk Factors

Screening

Natural History, Complications and Prognosis

Diagnosis

Diagnostic Study of Choice

History and Symptoms

Physical Examination

Laboratory Findings

Electrocardiogram

Chest X Ray

CT

MRI

Echocardiography or Ultrasound

Other Imaging Findings

Other Diagnostic Studies

Treatment

Medical Therapy

Surgery

Primary Prevention

Secondary Prevention

Cost-Effectiveness of Therapy

Future or Investigational Therapies

Case Studies

Case #1

Glucose-6-phosphate dehydrogenase deficiency pathophysiology On the Web

Most recent articles

Most cited articles

Review articles

CME Programs

Powerpoint slides

Images

American Roentgen Ray Society Images of Glucose-6-phosphate dehydrogenase deficiency pathophysiology

All Images
X-rays
Echo & Ultrasound
CT Images
MRI

Ongoing Trials at Clinical Trials.gov

US National Guidelines Clearinghouse

NICE Guidance

FDA on Glucose-6-phosphate dehydrogenase deficiency pathophysiology

CDC on Glucose-6-phosphate dehydrogenase deficiency pathophysiology

Glucose-6-phosphate dehydrogenase deficiency pathophysiology in the news

Blogs on Glucose-6-phosphate dehydrogenase deficiency pathophysiology

Directions to Hospitals Treating Glucose-6-phosphate dehydrogenase deficiency

Risk calculators and risk factors for Glucose-6-phosphate dehydrogenase deficiency pathophysiology

Overview

It is understood that G6PD deficiency is the result of reduced Glucose-6-phosphate dehydrogenase enzyme levels. G6PD deficiency is an X-linked disorder. Glucose-6-phosphate dehydrogenase enzyme oxidizes glucose-6-phosphate to 6-phosphogluconolactone in pentose phosphate pathway ( HMP shunt). Glucose-6-phosphate dehydrogenase enzyme also reduces nicotinamide adenine dinucleotide phosphate (NADP) to NADPH. NADPH is an important cofactor in glutathione metabolism against oxidative injury in RBC. In G6PD deficiency, oxidative stresses can denature hemoglobin and intravascular hemolysis in RBC can happen. The gene G6PD is located in the distal long arm of the X chromosome at the Xq28 locus. G6PD B, is the wild type or normal. On microscopic histopathological analysis, Heinz bodies can be visualized as a result of denatured hemoglobin in peripheral blood smears with supravital staining.

Pathophysiology

Physiology

The normal physiology of G6PD deficiency can be understood as follows:

Mechanism of G6PD
Mechanism of G6PD



















Pathogenesis

Genetics

G6PD deficiency is transmitted in x-linked disorder pattern. The gene G6PD is located in the distal long arm of the X chromosome at the Xq28 locus. [1]

Heterozygous women are usually normal because of lyonization ( X innactivation)[2]

G6PD B, is the wild type or normal. G6PD has 400 variant enzymes. [3] Caucasians, Asians and majority of blacks has G6PD B.

G6PD A+: In Africa, in 20-30 percent of black. In this variant, asparagine is substitued for aspartate, at amino acid 126. [4] It has normal enzyme activity.

The development of G6PD deficency is the result of missense point mutations and also a few deletions. [5]

  • G6PD A+:In Africa, in 20-30 percent of black. In this variant, asparagine is substitued for aspartate, at amino acid 126. [4] It has normal enzyme activity.
  • G6PD A-: Cause primaquine sensitivity in blacks.
  • G6PD mediterranean variant: Single base substitution (C—>T) at nucleotide 563 [6]
  • G6PD variants in Asia:
    • In China: G6PD Canton (1376 G—>T), G6PD Kaiping (1388 G—>A), G6PD Gaohe (95 G—>A)[7]
    • In Southeast Asia: G6PD Mahidol (487G—>A)

Associated Conditions

Gross Pathology

On gross pathology,there are no characteristic findings of G6PD deficiency.

Microscopic Pathology

On microscopic histopathological analysis, Heinz bodies can be visualized as a result of denatured hemoglobin in peripheral blood smears with supravital staining. (Heinz body prep).[10]

Heinz bodies , via wikipedia.org[11]



















References

  1. ↑ KIRKMAN HN, HENDRICKSON EM (September 1963). "Sex-linked electrophoretic difference in glucose-6-phosphate dehydrogenase". Am. J. Hum. Genet. 15: 241–58. PMC 1932381. PMID 14033020.
  2. ↑ BEUTLER E, YEH M, FAIRBANKS VF (January 1962). "The normal human female as a mosaic of X-chromosome activity: studies using the gene for C-6-PD-deficiency as a marker". Proc. Natl. Acad. Sci. U.S.A. 48: 9–16. PMC 285481. PMID 13868717.
  3. ↑ Beutler E (December 1994). "G6PD deficiency". Blood. 84 (11): 3613–36. PMID 7949118.
  4. ↑ 4.0 4.1 Yoshida A (March 1967). "A single amino Acid substitution (asparagine to aspartic Acid) between normal (b+) and the common negro variant (a+) of human glucose-6-phosphate dehydrogenase". Proc. Natl. Acad. Sci. U.S.A. 57 (3): 835–40. PMC 335583. PMID 16591538.
  5. ↑ Beutler E (April 1990). "The genetics of glucose-6-phosphate dehydrogenase deficiency". Semin. Hematol. 27 (2): 137–64. PMID 2190319.
  6. ↑ Vulliamy TJ, D'Urso M, Battistuzzi G, Estrada M, Foulkes NS, Martini G, Calabro V, Poggi V, Giordano R, Town M (July 1988). "Diverse point mutations in the human glucose-6-phosphate dehydrogenase gene cause enzyme deficiency and mild or severe hemolytic anemia". Proc. Natl. Acad. Sci. U.S.A. 85 (14): 5171–5. PMC 281710. PMID 3393536.
  7. ↑ McCurdy PR, Kirkman HN, Naiman JL, Jim RT, Pickard BM (March 1966). "A Chinese variant of glucose-6-phosphate dehydrogenase". J. Lab. Clin. Med. 67 (3): 374–85. PMID 4379606.
  8. ↑ Nagel RL, Roth EF (September 1989). "Malaria and red cell genetic defects". Blood. 74 (4): 1213–21. PMID 2669996.
  9. ↑ Rostami-Far Z, Ghadiri K, Rostami-Far M, Shaveisi-Zadeh F, Amiri A, Rahimian Zarif B (2016). "Glucose-6-phosphate dehydrogenase deficiency (G6PD) as a risk factor of male neonatal sepsis". J Med Life. 9 (1): 34–38. PMC 5152609. PMID 27974910.
  10. ↑ Jacob HS (July 1970). "Mechanisms of Heinz body formation and attachment to red cell membrane". Semin. Hematol. 7 (3): 341–54. PMID 5425759.
  11. ↑ From en.wikipedia.org, Public Domain, <"https://commons.wikimedia.org/w/index.php?curid=">4647353

Template:WH Template:WS

Retrieved from "https://www.wikidoc.org/index.php?title=Glucose-6-phosphate_dehydrogenase_deficiency_pathophysiology&oldid=1499789"