Biochemical and Histochemical Studies on Purine Nucleoside Phosphorylase Activity in Human T-and B-Lymphocytes

概要

論文の詳細を見る
Primary immunodeficiencies with defects of purine salvage enzymes have been recently reported. The facts that adenosine deaminase (ADA) deficiency is associated with both Tand B-cell dysfunctions but that purine nucleoside phosphorylase (PNP) deficiency is associated with only T-cell dysfunction lead to a working hypothesis that each type of these immunodeficiencies might result from the difference of the regulatory mechanism on purine metabolism between Tand B-cells. In order to testify this hypothesis, PNP activities as well as ADA activities were determined in T- and B-cells obtained by rosette-forming with sheep red blood cells (E)and antibody and complement coated sheep red blood cells (EAC), respectively. The activities were assayed biochemically and by a newly developed histochemical method. PNP activity biochemically assayed with T-cells was about 3-times higher than that with B-cells. ADA activity in Tcells was about 2-times higher than that in B-cells. Histochemical PNP and ADA stainings showed higher activities in T-cells than B-cells. The difference of PNP staining activity between T- and B-cells was found to be larger than that of ADA staining activity. These results suggest that PNP is more necessary for the function of T-cells than B-cells. A part of uric acid in sera is derived from purine bases produced by lymphocyte. T-cells with higher PNP and ADA activities take a greater part in uric acid production than B-cells with low PNP and ADA activities.
Japanese Society of Gout and Nucleic Acid Metabolismの論文

Biochemical and Histochemical Studies on Purine Nucleoside Phosphorylase Activity in Human T-and B-Lymphocytes

スポンサーリンク

概要

著者

関連論文

スポンサーリンク