HUMAN ADENOSINE-DEAMINASE - STOICHIOMETRY OF THE ADENOSINE DEAMINASE-BINDING PROTEIN COMPLEX

被引:29
作者
DADDONA, PE [1 ]
KELLEY, WN [1 ]
机构
[1] UNIV MICHIGAN, SCH MED, DEPT BIOL CHEM, ANN ARBOR, MI 48109 USA
关键词
Adenosine deaminase; Binding protein; Cross link; Stoichiometry;
D O I
10.1016/0005-2795(79)90143-0
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
In many human tissues adenosine deaminase exists as a large MW 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. 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 MW consistent with the proposed 2:1 stoichiometry. Sedimentation equilibrium analyses reveal a native MW 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 MW estimates.
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页码:302 / 311
页数:10
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