Immunoreactive protein in adenosine deaminase deficient human lymphoblast cell lines.

作者: D A Wiginton , J J Hutton

DOI: 10.1016/S0021-9258(19)81097-9

关键词:

摘要: Adenosine deaminase (adenosine aminohydrolase, EC 3.5.4.4) was examined in human lymphoblast cell lines from normal and adenosine deaminase-deficient individuals as well heterozygous for deficiency. activity determined by a specific enzymatic assay compared to immunoreactive protein (or cross-reacting material) radioimmunoassay, order investigate mutations affecting deaminase. Two different antisera, raised goat rabbit against deaminase, had sensitivities apparent specificities when used radioimmunoassay. Rabbit antisera provided the most sensitive of enzyme, whereas antiserum detection mutant proteins. A wide range values ratio observed deficient lines, ranging near 23 times normal. The with high ratios appear contain large amounts catalytically defective or inactive protein. amount detected radioimmunoassay depends upon utilized, making much 50-fold difference. approximately half activity, thus have two. partially an unstable impaired activity. Immunoreactive visualized extracts several after electrophoresis transfer activated paper, labeling immunological probes autoradiography.

参考文章(30)
W P Schrader, A R Stacy, Purification and subunit structure of adenosine deaminase from human kidney. Journal of Biological Chemistry. ,vol. 252, pp. 6409- 6415 ,(1977) , 10.1016/S0021-9258(17)39973-8
James C Alwine, David J Kemp, Barbara A Parker, Jakob Reiser, Jaime Renart, George R Stark, Geoffrey M Wahl, None, [15] Detection of specific RNAs or specific fragments of DNA by fractionation in gels and transfer to diazobenzyloxymethyl paper Methods in Enzymology. ,vol. 68, pp. 220- 242 ,(1979) , 10.1016/0076-6879(79)68017-5
W.P. Schrader, F.J. Woodward, B. Pollara, Purification of an adenosine deaminase complexing protein from human plasma. Journal of Biological Chemistry. ,vol. 254, pp. 11964- 11968 ,(1979) , 10.1016/S0021-9258(19)86411-6
Hitoshi Akedo, Hiromu Nishihara, Kiyoko Shinkai, Keiko Komatsu, Satsuki Ishikawa, Multiple forms of human adenosine deaminase: I. Purification and characterization of two molecular species Biochimica et Biophysica Acta. ,vol. 276, pp. 257- 271 ,(1972) , 10.1016/0005-2744(72)90028-9
W P Schrader, A R Stacy, B Pollara, Purification of human erythrocyte adenosine deaminase by affinity column chromatography. Journal of Biological Chemistry. ,vol. 251, pp. 4026- 4032 ,(1976) , 10.1016/S0021-9258(17)33351-3
M B Van der Weyden, W N Kelley, Human adenosine deaminase. Distribution and properties. Journal of Biological Chemistry. ,vol. 251, pp. 5448- 5456 ,(1976) , 10.1016/S0021-9258(17)33080-6
Dennis A. Carson, J. E. Seegmiller, Randall Goldblum, Quantitative immunoassay of adenosine deaminase in combined immunodeficiency disease. Journal of Immunology. ,vol. 118, pp. 270- 273 ,(1977)
W N Kelley, P E Daddona, Human adenosine deaminase. Purification and subunit structure. Journal of Biological Chemistry. ,vol. 252, pp. 110- 115 ,(1977) , 10.1016/S0021-9258(17)32805-3
P.E. Daddona, M.A. Frohman, W.N. Kelley, Human adenosine deaminase and its binding protein in normal and adenosine deaminase-deficient fibroblast cell strains. Journal of Biological Chemistry. ,vol. 255, pp. 5681- 5687 ,(1980) , 10.1016/S0021-9258(19)70683-8
Joanne Finstad, Göran Kronvall, Ulysses S. Seal, Ralph C. Williams, Phylogenetic insight into evolution of mammalian Fc fragment of gamma G globulin using staphylococcal protein A. Journal of Immunology. ,vol. 104, pp. 140- 147 ,(1970)