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PMID: 518903 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Human adenosine deaminase. Stoichiometry of the adenosine deaminase-binding protein complex.

Biochimica et biophysica acta ·Vol. 580 ·No. 2 ·1979-10-24 ·Pages 302-11

Daddona PE, Kelley WN

Abstract

In many human tissues adenosine deaminase exists as a large molecular weight complex (large form) composed of adenosine deaminase and an adenosine deaminase binding protein. The molar ratio of adenosine deaminase to binding protein in this large form complex appears to be 2:1, respectively, based on several observations. Scatchard-type analysis of the binding of 125I-labeled adenosine deaminase to purified binding protein indicates that 2.15 mol of adenosine deaminase are bound to 1 mol of binding protein. Chemical cross-linking of 125I-labeled adenosine deaminase-binding protein complex (large form) with glutaraldehyde produces 6 cross-linked species with molecular weights consistent with the proposed 2 to 1 stoichiometry. Sedimentation equilibrium analyses reveal a native molecular weight of 300 890 for the adenosine deaminase-binding protein complex (large form), 37 500 for small form adenosine deaminase, and 213 300 for the binding protein. A 2:1 molar ratio of adenosine deaminase and binding protein in the large form complex is most consistent with these molecular weight estimates.

MeSH Terms
Adenosine Deaminase Carrier Proteins Chemical Phenomena Chemistry Erythrocytes/enzymology Humans Kidney/enzymology Molecular Weight Nucleoside Deaminases Protein Binding Ultracentrifugation
Chemicals
Carrier Proteins Nucleoside Deaminases Adenosine Deaminase
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Daddona P E
Kelley W N
Article Info
Journal
Biochimica et biophysica acta
Abbr.
Biochim Biophys Acta
ISSN
0006-3002
Published
1979-10-24
Pages
302-11
Language
English
Region
Netherlands
NLM ID
0217513
Subset
IM
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