Sg. Sharoyan et al., ISOLATION, PURIFICATION, AND COMPARATIVE CHARACTERISTICS OF ADENOSINE-DEAMINASE FROM 5 BOVINE BRAIN-TISSUE FRACTIONS, Biochemistry, 59(2), 1994, pp. 169-174
Adenosine deaminase was isolated and purified from five brain tissue f
ractions: white and gray matters of the large hemispheres, cerebellum,
medulla oblongata, and pituitary anterior lobe. The pH optimum, K-m,
molecular weight, yield, and specific activities were determined for e
ach of the enzyme preparations. Differences in the enzyme from the var
ious brain tissues were observed by gel filtration and electrophoresis
. Bivalent copper ions (Cu2+) were shown to irreversibly inhibit the a
ctivity of the enzyme. Studies on the effect of sulfhydryl reagents su
ggest that sulfhydryl groups are not essential for the catalytic activ
ity of adenosine deaminase.