PMID: 6977542Mar 25, 1982Paper

Immunoreactive protein in adenosine deaminase deficient human lymphoblast cell lines.

The Journal of Biological Chemistry
D A Wiginton, J J Hutton

Abstract

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 as individuals heterozygous for adenosine deaminase deficiency. Adenosine deaminase activity was determined by a specific enzymatic assay and compared to immunoreactive adenosine deaminase protein (or cross-reacting material) determined by radioimmunoassay, in order to investigate mutations affecting adenosine deaminase. Two different antisera, raised in goat and rabbit against human adenosine deaminase, had different sensitivities and apparent specificities when used for radioimmunoassay. Rabbit antisera provided the most sensitive assay of normal enzyme, whereas goat antiserum provided the most sensitive assay for detection of mutant proteins. A wide range of values for the ratio of immunoreactive protein to activity was observed for the adenosine deaminase deficient cell lines, ranging from near normal to 23 times normal. The cell lines with high ratios appear to contain large amounts of catalytically defective or inactive protein. The amount of mutant protein detected by radioimmunoassay in the deficient cell lines depends upon the antiserum utilized, makin...Continue Reading

Related Concepts

Related Feeds

ASBMB Publications

The American Society for Biochemistry and Molecular Biology (ASBMB) includes the Journal of Biological Chemistry, Molecular & Cellular Proteomics, and the Journal of Lipid Research. Discover the latest research from ASBMB here.