Purification of an adenosine deaminase complexing protein from human plasma.
نویسندگان
چکیده
منابع مشابه
Localization of adenosine deaminase and adenosine deaminase complexing protein in rabbit heart. Implications for adenosine metabolism.
The distribution of adenosine deaminase and adenosine deaminase complexing protein in rabbit heart has been compared using immunohistochemical staining procedures. Sections (4-5 microns) of tissue fixed in Clarke's solution or paraformaldehyde and embedded in paraffin were stained by the peroxidase anti-peroxidase method for adenosine deaminase or complexing protein, using affinity purified ant...
متن کاملCharacterization of the adenosine deaminase-adenosine deaminase complexing protein binding reaction.
Glutaraldehyde-fixed membranes from rabbit kidney cortex were used to characterize binding of monomeric adenosine deaminase to the adenosine deaminase complexing protein. With the use of bovine adenosine deaminase it was shown that enzyme binding is a saturable, high affinity process. The K value for binding of the bovine enzyme was 11 nM. Maximum enzyme binding and rate of binding to a constan...
متن کاملHuman Adenosine Deaminase Binding Protein
In many human tissues adenosine deaminase exists as a complex composed of two proteins; one protein has adenosine deaminase activity while the other represents a binding protein with no other known binding activity. A rapid, quantitative assay for human adenosine deaminase binding protein has been developed utilizing ‘251-labeled calf adenosine deaminase. In addition this binding protein has be...
متن کاملPurification of human erythrocyte adenosine deaminase by affinity column chromatography.
Adenosine deaminase (adenosine aminohydrolase EC 3.5.4.4) has been purified 468,000-fold from pooled human erythrocytes. The procedure developed was used to isolate the enzyme from up to 23 liters of packed erythrocytes at one time. An easily prepared affinity column bed material employing adenosine as the ligand was used as the final step in the purification. During elution from the affinity c...
متن کاملClustered charged amino acids of human adenosine deaminase comprise a functional epitope for binding the adenosine deaminase complexing protein CD26/dipeptidyl peptidase IV.
Human adenosine deaminase (ADA) occurs as a 41-kDa soluble monomer in all cells. On epithelia and lymphoid cells of humans, but not mice, ADA also occurs bound to the membrane glycoprotein CD26/dipeptidyl peptidase IV. This "ecto-ADA" has been postulated to regulate extracellular Ado levels, and also the function of CD26 as a co-stimulator of activated T cells. The CD26-binding site of human AD...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1979
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)86411-6