scholarly journals Evaluation of adenosine deaminase and other purine salvage pathway enzymes in horses with combined immunodeficiency.

1976 ◽  
Vol 13 (3) ◽  
pp. 995-997 ◽  
Author(s):  
T C McGuire ◽  
B Pollara ◽  
J J Moore ◽  
M J Poppie

2006 ◽  
Vol 71 (6) ◽  
pp. 769-787 ◽  
Author(s):  
Mukta Gupta ◽  
Vasu Nair

Adenosine deaminase (ADA) is an enzyme in the purine salvage pathway that catalyzes the deamination of adenosine and deoxyadenosine to inosine and deoxyinosine, respectively. This deamination is an important factor in limiting the usefulness of adenosine analogues in chemotherapy. However, the biocatalysis by ADA is also a useful transformation in enzymatic synthesis. In this review, examples from both the principal investigator's laboratory and from the literature, which depict the synthetic usefulness of this enzyme in deamination, dehalogenation, demethoxylation reactions and in diastereoisomeric resolution, are presented. It is not the intent of this review to comprehensively list all of the biotransformations induced by adenosine deaminase, but rather to present representative examples to highlight the powerful synthetic utility of this enzyme. A review with 72 references.



2018 ◽  
Vol 37 (2) ◽  
pp. 128-133 ◽  
Author(s):  
Mina Ebrahimi-Rad ◽  
Shohreh Khatami ◽  
Shahla Ansari ◽  
Shohreh Jalylfar ◽  
Shirin Valadbeigi ◽  
...  

SummaryBackground:Acute lymphoblastic leukemia (ALL) is known as the most prevalent pediatric malignancy all around the world. Identification of specific biomarker is necessary for early diagnosis and effective therapy. It is believed that Adenosine deaminase (ADA) as an enzyme involved in the purine salvage pathway increases in ALL patients. Herein, the quantity and pattern of ADA isoenzymes were surveyed among ALL patients in comparison to healthy subjects.Methods:Serum and RBC samples of three different groups of ALL patients, including newly diagnosed cases without any drugs administration, subjects with the relapsed disease, patients in the remission stage after therapy, and the healthy subjects were enrolled in the study. Then, the activity and pattern of ADA1, ADA2 and ADA1+cp were determined using ADA kit and electrophoresis on SDS-PAGE, respectively. To confirm the presence of ADA enzyme, the fresh serums, extractions from erythrocytes, JM cell line as a human T lymphocyte line and J774 A.1 as mouse monocyte line were electrophoresed on 1.2% agarose gel and stained with the specific dye.Results:The activities of ADA1 isoenzyme and total ADA in new cases and subjects with the relapsed disease were significantly higher than their activities in the patients in the remission stage and healthy controls (p<0.001). The unbounded ADA1 isoenzyme was found to exist in the erythrocyte, lymphocyte and monocyte. But in serum, all the ADA1 was bounded to the cp protein.Conclusions:ADA1 is the key isoenzyme elevating in ALL patients, therefore this isoenzyme could be a useful biomarker to diagnose ALL patients and monitor their therapies.







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