scholarly journals Anemia due to Erythrocyte Enzyme Disorder

2020 ◽  
Author(s):  
Keyword(s):  
Erythrocyte Enzyme

Distribution of some erythrocyte enzyme polymorphisms in Emilia Romagna (Northern Italy)

1995 ◽  
Vol 80 (3) ◽  
pp. 371-376
Author(s):  
Maria Fuciarelli ◽  
Emilia Paba ◽  
Hubert Walter ◽  
Gian Franco De Stefano
Keyword(s):  
Northern Italy ◽  
Enzyme Polymorphisms ◽  
Erythrocyte Enzyme

scholarly journals Selenium-dependent glutathione peroxidase protein and activity: immunological investigations on cellular and plasma enzymes

Blood ◽  
1986 ◽  
Vol 68 (3) ◽  
pp. 640-645 ◽  
Author(s):  
K Takahashi ◽  
HJ Cohen
Keyword(s):  
Enzyme Activity ◽  
Glutathione Peroxidase ◽  
Protein Content ◽  
Polyclonal Antibodies ◽  
Plasma Enzyme ◽  
Plasma Enzymes ◽  
Erythrocyte Enzyme ◽  
Dependent Protein ◽  
Gshpx Activity ◽  
Almost All

Selenium-deficient humans and animals are known to be deficient in glutathione peroxidase (GSHPx) activity in their cells and plasma. To determine the relationship between enzyme activity and protein content, the enzyme was purified from human erythrocytes, and polyclonal antibodies were made against the purified protein in rabbits. These antibodies were found to be monospecific, noninhibitory, and capable of precipitating the enzymatic activity. All the GSHPx activity in erythrocytes and almost all the activity in neutrophils and platelets was precipitated by these antibodies. None of the plasma enzyme was precipitated by these antibodies, indicating that the plasma enzyme activity was attributable to a different selenium dependent protein moiety. Utilizing a radioimmunoassay, we were able to determine that there was a direct relationship between GSHPx activity and protein content in the erythrocytes of both normal and selenium-deficient individuals, and a similar relationship between control and selenium- deficient rat erythrocytes and liver cells. Thus, the ability to examine GSHPx as a protein resulted in two new observations concerning the selenium-dependent GSHPx. The first is that the plasma enzyme is antigenically distinct from the erythrocyte enzyme, and the second is that in the absence of selenium, there is a concomitant decrease in GSHPx protein.

On the diagnosis of erythrocyte enzyme defects in the presence of high reticulocyte counts

1989 ◽  
Vol 72 (3) ◽  
pp. 445-451 ◽  
Author(s):  
M. Lakomek ◽  
W. Schröter ◽  
G. Maeyer ◽  
H. Winkler
Keyword(s):  
Erythrocyte Enzyme ◽  
Enzyme Defects

scholarly journals Mechanisms of adenosine 5'-monophosphate catabolism in human erythrocytes

Blood ◽  
1986 ◽  
Vol 67 (4) ◽  
pp. 988-992 ◽  
Author(s):  
DE Paglia ◽  
WN Valentine ◽  
M Nakatani ◽  
RA Brockway
Keyword(s):  
Potential Role ◽  
Adenine Nucleotide ◽  
Acidic Ph ◽  
Amp Deaminase ◽  
Severe Deficiency ◽  
Erythrocyte Enzyme ◽  
Senescent Erythrocytes ◽  
Adenine Nucleotide Pool ◽  
Normal Controls

Abstract Uncertainties regarding the role of pyrimidine nucleotidase (PyrNase) in AMP catabolism were resolved by studies of erythrocytes from normal controls, controls with young mean cell ages, and patients with hereditary hemolytic anemia due to severe deficiency of PyrNase. Hemolysates from the latter exhibited undiminished capacity to dephosphorylate AMP over a broad range of pH, indicating that PyrNase was not directly involved. In each subject group, the rates of AMP dephosphorylation between pH 5.1 and 8.3 were indistinguishable from those of IMP, suggesting a potential role for AMP-deaminase, an erythrocyte enzyme that was stimulated by coformycin at pH 7.2. Quantitative analysis of catabolites in incubated hemolysates confirmed that AMP degradation preferentially occurred via deamination to IMP with subsequent dephosphorylation by another erythrocyte nucleotidase isozyme, deoxyribonucleotidase. Both AMP-deaminase and deoxyribonucleotidase have acidic pH optima with minimal activities at physiologic pH, suggesting that this pathway of AMP catabolism could accelerate depletion of the adenine nucleotide pool and thereby mediate the demise of senescent erythrocytes sequestered in the spleen.

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