Summary
A specific competitive radioimmunoassay (RIA) was employed to quantify human adenosine deaminase molecules produced in human-Chinese hamster somatic cell hybrids. Studies on a set of hybrids in which the normal and aberrant expressions of adenosine deaminase (assigned earlier to human chromosome 20) were segregating, have demonstrated that in the patient with ADA -SCID disease reported by Herbschleb-Voogt et al (1981a), the deficiency of ADA activity was associated with a comparable deficiency of adenosine deaminase specific immuno-crossreacting material (ADA-CRM).
Similar content being viewed by others
References
Arvidson S, Holme T, Wadström T (1971) Influence of cultivation conditions on the production of extracellular proteins by Staphylococcus aureus Acta Pathol Microbiol Scand [B] 79:399–405
Carson DA, Goldblum R, Seegmiller JE (1977) Quantitative immunoassay of adenosine deaminase in combined immunodeficiency disease. J Immunol 118:270–273
Chechik BE, Madapallimattam A, Gelfand E (1979) Radioimmunoassay for human thymus-leukemia associated antigen. J Natl Cancer Inst 62:465–470
Chechik BE, Schrader WP, Daddona PE (1980) Identification of human thymus-leukemia associated antigen as a low molecular weight form of adenosine deaminase. J Natl Cancer Inst 64:1077–1083
Cullen SE, Schwartz BD (1976) An improved method for isolation of H-2 and Ia alloantigens with immunoprecipitation induced by protein A-bearing staphylococci. J Immunol 117:136–142
Daddona PE, Frohman MA, Kelley WN (1979) Radioimmunochemical quantitation of human adenosine deaminase. J Clin Invest 64: 798–803
Daddona PE, Frohman MA, Kelley WN (1980) Human adenosine deaminase and its binding protein in normal and adenosine deaminase-deficient fibroblast cell strains. J Biol Chem 255: 5681–5687
Ghangas GS, Milman G (1975) Radioimmune determination of hypoxanthine phosphoribosyltransferase cross-reacting material in erythrocytes of Lesch-Nyhan patients. Proc Natl Acad Sci USA 72:4147–4150
Gray GM, Conklin DA, Townley RRW (1976) Sucrose-isomaltase deficiency. Absence of an inactive enzyme variant. N Engl J Med 294:750–753
Hamers MN, Westerveld A, Meera Khan P, Tager JM (1977) Characterization of α-galactosidase isozymes in normal and Fabry human-Chinese hamster somatic cell hybrids. Hum Genet 36:289–297
Held KR, Kahan B, DeMars R (1975) Adenine phosphoribosyltransferase and hypoxanthine-guanine phosphoribosyltransferase immunoprecipitation reactions in human-mouse and human-Chinese hamster cell hybrids. Hum Genet 30:23–34
Herbschleb-Voogt E, Pearson PL, Vossen JM, Meera Khan P (1981a) Basic defect in the expression of adenosine deaminase in ADA -SCID disease investigated through the cells of an obligate heterozygote. Hum Genet 56:379–386
Herbschleb-Voogt E, Grzeschik K-H, Pearson PL, Meera Khan P (1981b) Assignment of adenosine deaminase complexing protein (ADCP) gene(s) to human chromosome 2 in rodent-human somatic cell hybrids. Hum Genet 59:317–323
Herbschleb-Voogt E, Kate J ten, Meera Khan P (1983) Adenosine deaminase complexing protein (ADCP): A transformation sensitive protein with potentials of a cancer marker. Anticancer Res 3:
Hoeksema HL, de Wit J, Westerveld A (1980) The genetic defect in various types of human β-galactosidase deficiency. Hum Genet 53: 241–247
Hopkinson DA, Cook PJL, Harris H (1969) Further data on the adenosine deaminase polymorphism and a report of a new phenotype. Ann Hum Genet 32:361–367
Lowry OH, Rosebrough NJ, Farr AL, Randall RJ (1951) Protein measurement with the Folin phenol reagent. J Biol Chem 193: 265–275
Pharmacia Fine Chemicals Uppsala (1979) Affinity chromatography. Principles and methods. Ljungföretagen. Örebro, pp 15–18
Rodbard D, Bridson W, Rayford PL (1969) Rapid calculation of radioimmunoassay results. J Lab Clin Med 74:770–781
Rossi CA, Lucacchini A, Montali V, Ronca G (1975) A general method of purification of adenosine deaminase by affinity chromatography. Int J Pept Protein Res 7:81–89
Schrader WP, Stacy AR, Pollara B (1976) Purification of human erythrocyte adenosine deaminase by affinity chromatography. J Biol Chem 251:4026–4032
Trotta PP, Smithwick EM, Balis ME (1976) A normal level of adenosine deaminase activity in the red cell lysates of carriers and patients with severe combined immunodeficiency disease. Proc Natl Acad Sci USA 73:104–108
Van Kampen EJ, Zijlstra WG (1961) Standardization of hemoglobinometry. II. The hemiglobincyanide method. Clin Chim Acta 6: 538–544
Weatherall DJ, Clegg JB (1982) Thalassemia revisited. Cell 29:7–9
Weber K, Osborn M (1969) The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis. J Biol Chem 244:4406–4412
Wiginton DA, Hutton JJ (1982) Immunoreactive protein in adenosine deaminase deficient lymphoblastoid cell lines. J Biol Chem 257: 3211–3217
Author information
Authors and Affiliations
Additional information
Part I of this study has been reported earlier (Hum Genet 56:379–386, 1981)
Rights and permissions
About this article
Cite this article
Herbschleb-Voogt, E., Scholten, JW. & Khan, P.M. Basic defect in the expression of adenosine deaminase in ADA -SCID disease. Hum Genet 63, 121–125 (1983). https://doi.org/10.1007/BF00291530
Received:
Issue Date:
DOI: https://doi.org/10.1007/BF00291530