Results 161 to 170 of about 29,706 (209)
Some of the next articles are maybe not open access.
Adenosine deaminase and purinergic neuroregulation
Neurochemistry International, 1990During the early 1970s purines and their associated enzymes were largely believed to be ubiquitous and evenly distributed throughout neural tissues. There is now firm immunohistochemical and neurochemical evidence that this is not the case for the catabolic enzyme adenosine deaminase (ADA) nor is it true for adenosine transport sites labelled by the ...
J I, Nagy, J D, Geiger, W A, Staines
openaire +2 more sources
The linkage relationships of adenosine deaminase
Annals of Human Genetics, 1970SUMMARYThe lod scores for seventy‐six families segregating for adenosine deaminase have been estimated. Taken in conjunction with other published lod scores there is a suggestion that ADA may be linked with P.
P J, Cook, D A, Hopkinson, E B, Robson
openaire +2 more sources
Adenosine and Adenosine Deaminase Contrary Manifestations in Immunity
Scandinavian Journal of ImmunologyABSTRACTAdenosine (Ado) is an important purine that regulates numerous physiological functions. Adenosine deaminase (ADA) catalyses the irreversible deamination of Ado and its derivatives. Ado and ADA are the essential players in the immune system, but their roles often are opposite, mutually exclusive and competitive.
Sona Mardanyan +2 more
openaire +2 more sources
Methods in enzymology, 1977
Adenosine deaminase plays a key role in adenosine metabolism. This nueleoside has some important pharmacological and toxic effects. An adenosine deaminase deficiency observed in some cases of severe congenital immunodeficiency represents the first link between an immunological and enzymic defect.
Ronca G +2 more
openaire +2 more sources
Adenosine deaminase plays a key role in adenosine metabolism. This nueleoside has some important pharmacological and toxic effects. An adenosine deaminase deficiency observed in some cases of severe congenital immunodeficiency represents the first link between an immunological and enzymic defect.
Ronca G +2 more
openaire +2 more sources
Treatment of Adenosine Deaminase Deficiency
BioDrugs, 1998Severe combined immune deficiency disease due to a deficiency of the enzyme adenosine deaminase is a rare disease. However, it has been used as a prototype disease for the development of a variety of treatment modalities that are currently applied in more frequent diseases.
P M, Hoogerbrugge +3 more
openaire +2 more sources
Adenosine deaminase isozymes in Artemia
Comparative Biochemistry and Physiology Part B: Comparative Biochemistry, 1984Three isozymes of adenosine deaminase, termed II, III and IV, have been detected in Artemia embryos. Their pI values, determined by chromatofocusing, were 4.9, 5.0 and 5.2, respectively. Upon development to larvae, a different isozyme (I) is induced, with a pI value of 4.2 as determined by isoelectric focusing.
A, Fernández +5 more
openaire +2 more sources
Adenosine Deaminase and Thymocyte Maturation
Scandinavian Journal of Immunology, 1991The congenital absence of adenosine deaminase in humans results in severe combined immunodeficiency. To clarity the process whereby thymocytes are destroyed in the absence of adenosine deaminase activity, we induced a parallel condition in mice through the injection of an inhibitor of adenosine deaminase, deoxycoformycin.
P J, Doherty +7 more
openaire +2 more sources
Erythrocyte Adenosine Deaminase in Malaysians
Human Heredity, 1975944 adenosine deaminase phenotypings of Malay, Chinese, and Indian blood donors and newborns at Kuala Lumpur, Malaysia, yielded ADA1 gene frequency estimates of 0.885 for the Malays, 0.939 for the Chinese, and 0.853 for the Indians.
Q B, Welch, L E, Lie-Injo, J, Ganesan
openaire +2 more sources
Nihon rinsho. Japanese journal of clinical medicine, 1995
Adenosine deaminase (adenosine aminohydrolase, EC 3.5.4.4; ADA) activity is widely distributed in human tissues and is highest in lymphoid tissues. Two ADA isozymes are known as ADA1 and ADA2. Human tissue extracts contained ADA1 predominantly. Meanwhile, ADA2 was the main component of serum ADA. ADA activity was significantly elevated in the sera from
openaire +1 more source
Adenosine deaminase (adenosine aminohydrolase, EC 3.5.4.4; ADA) activity is widely distributed in human tissues and is highest in lymphoid tissues. Two ADA isozymes are known as ADA1 and ADA2. Human tissue extracts contained ADA1 predominantly. Meanwhile, ADA2 was the main component of serum ADA. ADA activity was significantly elevated in the sera from
openaire +1 more source
The adenosine deaminase of crustaceans
Biochimica et Biophysica Acta, 1956A H, ROUSH, R F, BETZ
openaire +2 more sources