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Genetic polymorphism of esterase B3 in human leukocytes
1Joseph Stokes, Jr. Research Institute, Children's Hospital of Philadelphia, PA.
Annals of Human Genetics
|July 1, 1986
Summary
A genetic variant of the human enzyme esterase B3 (ESB3) was identified in leukocytes. This variant, inherited as a Mendelian trait, affects the enzyme's trimeric structure.
Area of Science:
- Biochemistry
- Human Genetics
- Enzymology
Background:
- Human tissues possess esterase activity, including ESB3, detectable via electrophoresis and specific staining.
- Previous studies have characterized ESB3 enzyme activity and its detection methods.
Purpose of the Study:
- To identify and characterize electrophoretic variants of the human ESB3 enzyme.
- To investigate the inheritance pattern and molecular basis of an observed ESB3 variant.
Main Methods:
- Starch gel electrophoresis of mononuclear leukocytes.
- Staining with alpha-naphthyl butyrate to detect esterase activity.
- Family studies to analyze inheritance patterns.
Main Results:
- An electrophoretic variant of ESB3 was identified in mononuclear leukocytes.
- The variant (ESB3 2-1 phenotype) is inherited as a simple Mendelian trait, with the ESB3(2) allele frequency at 0.035 in U.S. Whites.
- The ESB3(2) allele mutation affects subunit assembly into the trimeric enzyme structure without altering charge.
Conclusions:
- A novel genetic variant of human ESB3 esterase has been characterized.
- The ESB3(2) allele provides insight into enzyme structure-function relationships and subunit assembly.
- Further research is warranted to fully understand the implications of this genetic variation.