Skip to main content
NCBI home page
The Journal of Clinical Investigation logoLink to The Journal of Clinical Investigation
. 1965 Mar;44(3):486–493. doi: 10.1172/JCI105162

Complete Pseudocholinesterase Deficiency: Genetic and Immunologic Characterization*

W E Hodgkin 1,2,3,4,†, E R Giblett 1,2,3,4, H Levine 1,2,3,4, W Bauer 1,2,3,4, A G Motulsky 1,2,3,4,‡
PMCID: PMC292499  PMID: 14271308

Full text

PDF
486

Images in this article

489Image
on p.489

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. AEBI H., BAGGIOLINI M., DEWALD B., LAUBER E., SUTER H., MICHELI A., FREI J. OBSERVATIONS IN TWO SWISS FAMILIES WITH ACATALASIA. II. Enzymol Biol Clin (Basel) 1964;74:121–151. doi: 10.1159/000458023. [DOI] [PubMed] [Google Scholar]
  2. CLITHEROW J. W., MITCHARD M., HARPER N. J. THE POSSIBLE BIOLOGICAL FUNCTION OF PSEUDOCHOLINESTERASE. Nature. 1963 Sep 7;199:1000–1001. doi: 10.1038/1991000a0. [DOI] [PubMed] [Google Scholar]
  3. DOENICKE A., GURTNER T., KREUTZBERG G., REMES I., SPIESS W., STEINBEREITHNER K. Serum cholinesterase anenzymia. Report of a case confirmed by enzyme-histochemical examination of liver-biopsy specimen. Acta Anaesthesiol Scand. 1963;7:59–68. doi: 10.1111/j.1399-6576.1963.tb00204.x. [DOI] [PubMed] [Google Scholar]
  4. HARRIS H., HOPKINSON D. A., ROBSON E. B. Two-dimensional electrophoresis of pseudocholinesterase components in normal human serum. Nature. 1962 Dec 29;196:1296–1298. doi: 10.1038/1961296a0. [DOI] [PubMed] [Google Scholar]
  5. HARRIS H., WHITTAKER M. Differential inhibition of human serum cholinesterase with fluoride: recognition of two new phenotypes. Nature. 1961 Jul 29;191:496–498. doi: 10.1038/191496a0. [DOI] [PubMed] [Google Scholar]
  6. HARRIS H., WHITTAKER M., LEHMANN H., SILK E. The pseudocholinesterase variants. Esterase levels and dibucaine numbers in families selected through suxamethonium sensitive individuals. Acta Genet Stat Med. 1960;10:1–16. doi: 10.1159/000151112. [DOI] [PubMed] [Google Scholar]
  7. HARRIS H., WHITTAKER M. The serum cholinesterase variants. A study of twenty-two families selected via the 'intermediate' phenotype. Ann Hum Genet. 1962 Jul;26:59–72. doi: 10.1111/j.1469-1809.1962.tb01310.x. [DOI] [PubMed] [Google Scholar]
  8. JACOB F., MONOD J. Genetic regulatory mechanisms in the synthesis of proteins. J Mol Biol. 1961 Jun;3:318–356. doi: 10.1016/s0022-2836(61)80072-7. [DOI] [PubMed] [Google Scholar]
  9. KALOW W., GENEST K. A method for the detection of atypical forms of human serum cholinesterase; determination of dibucaine numbers. Can J Biochem Physiol. 1957 Jun;35(6):339–346. doi: 10.1139/y57-041. [DOI] [PubMed] [Google Scholar]
  10. KALOW W., GUNN D. R. Some statistical data on atypical cholinesterase of human serum. Ann Hum Genet. 1959 Jul;23:239–250. doi: 10.1111/j.1469-1809.1959.tb01467.x. [DOI] [PubMed] [Google Scholar]
  11. KALOW W., LINDSAY H. A. A comparison of optical and manometric methods for the assay of human serum cholinesterase. Can J Biochem Physiol. 1955 Jul;33(4):568–574. [PubMed] [Google Scholar]
  12. KALOW W., STARON N. On distribution and inheritance of atypical forms of human serum cholinesterase, as indicated by dibucaine numbers. Can J Biochem Physiol. 1957 Dec;35(12):1305–1320. [PubMed] [Google Scholar]
  13. LERNER P., YANOFSKY C. An immunological study of mutants of Escherichia coli lacking the enzyme tryptophan synthetase. J Bacteriol. 1957 Oct;74(4):494–501. doi: 10.1128/jb.74.4.494-501.1957. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. LIDDELL J., LEHMANN H., DAVIES D., SHARIH A. Physical separation of pseudocholinesterase variants in human serum. Lancet. 1962 Mar 3;1(7227):463–464. doi: 10.1016/s0140-6736(62)91423-x. [DOI] [PubMed] [Google Scholar]
  15. LIDDELL J., LEHMANN H., SILK E. A 'silent' pseudo-cholinesterase gene. Nature. 1962 Feb 10;193:561–562. doi: 10.1038/193561a0. [DOI] [PubMed] [Google Scholar]
  16. NISHIMURA E. T., KOBARA T. Y., TAKAHARA S., HAMILTON H. B., MADDEN S. C. Immunologic evidence of catalase deficiency in human hereditary acatalasemia. Lab Invest. 1961 Mar-Apr;10:333–340. [PubMed] [Google Scholar]
  17. POULIK M. D. Starch gel electrophoresis in a discontinous system of buffers. Nature. 1957 Dec 28;180(4600):1477–1479. doi: 10.1038/1801477a0. [DOI] [PubMed] [Google Scholar]
  18. SIMPSON N. E., KALOW W. THE "SILENT" GENE FOR SERUM CHOLINESTERASE. Am J Hum Genet. 1964 Jun;16:180–188. [PMC free article] [PubMed] [Google Scholar]
  19. SMITHIES O. An improved procedure for starch-gel electrophoresis: further variations in the serum proteins of normal individuals. Biochem J. 1959 Mar;71(3):585–587. doi: 10.1042/bj0710585. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. STENT G. S. THE OPERON: ON ITS THIRD ANNIVERSARY. MODULATION OF TRANSFER RNA SPECIES CAN PROVIDE A WORKABLE MODEL OF AN OPERATOR-LESS OPERON. Science. 1964 May 15;144(3620):816–820. doi: 10.1126/science.144.3620.816. [DOI] [PubMed] [Google Scholar]
  21. SUSKIND S. R., WICKHAM M. L., CARSIOTIS M. Antienzymes in immunogenetic studies. Ann N Y Acad Sci. 1963 May 8;103:1106–1127. doi: 10.1111/j.1749-6632.1963.tb53762.x. [DOI] [PubMed] [Google Scholar]
  22. Suskind S. R., Yanofsky C., Bonner D. M. ALLELIC STRAINS OF Neurospora LACKING TRYPTOPHAN SYNTHETASE: A PRELIMINARY IMMUNOCHEMICAL CHARACTERIZATION. Proc Natl Acad Sci U S A. 1955 Aug 15;41(8):577–582. doi: 10.1073/pnas.41.8.577. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. TAKAHARA S., OGATA M., KOBARA T. Y., NISHIMURA E. T., BROWN W. J. The "catalase protein" of acatalasemic red blood cells. An electrophoretic and immunologic study. Lab Invest. 1962 Sep;11:782–790. [PubMed] [Google Scholar]
  24. URIEL J. Characterization of enzymes in specific immuneprecipitates. Ann N Y Acad Sci. 1963 May 8;103:956–979. doi: 10.1111/j.1749-6632.1963.tb53748.x. [DOI] [PubMed] [Google Scholar]
  25. WOOLF L. I. Gene expression in heterozygotes. Nature. 1962 May 12;194:609–610. doi: 10.1038/194609a0. [DOI] [PubMed] [Google Scholar]

Articles from Journal of Clinical Investigation are provided here courtesy of American Society for Clinical Investigation

RESOURCES