Abstract
Although the electrophoretic mobility of HeLa G6PD is similar to that of the common Negro variant G6PD A+, several reports have suggested slight differences between HeLa G6PD and G6PD A+. This study, carried out using the pure homogeneous B+, A+, and HeLa G6PD, showed that (1) the electrophoretic mobility of HeLa G6PD is identical to that of G6PD A+, (2) the enzymatic properties and thermostability of HeLa G6PD are indistinguishable from those of G6PD A+, and (3) the peptide map of the tryptic digest of HeLa G6PD is identical to that of G6PD A+, with one peptide spot of HeLa G6PD different from the corresponding spot of G6PD B+. These results indicate that the structure of HeLa G6PD is identical to that of G6PD A+, and that the amino acid substitution in HeLa G6PD is from one asparagine residue in the wild-type G6PD B+ to an aspartic acid residue in HeLa G6PD.
This is a preview of subscription content, log in via an institution to check access.
Similar content being viewed by others
References
Auersperg, N., and Gartler, S. M. (1970). Isoenzyme stability in human heteroploid cell lines. Exptl. Cell Res. 61 465.
Gartler, S. M. (1967). Genetic Markers as Tracers in Cell Culture, National Cancer Institute Monograph No. 26, p. 167.
Hathaway, P., and La Rock, J. F. (1969). HeLa G6PD differs from G6PD A+. Abstracts, Annual Meeting of the American Society for Human Genetics, p. 25.
Motulsky, A. G., and Yoshida, A. (1969). Methods for the study of red cell glucose-6-phosphate dehydrogenase. In Yunis, J. J. (ed.), Biochemical Methods in Red Cell Genetics, Academic Press, New York, p. 51.
Rattazzi, M. C., and Siniscalco, M. (1969). Electrophoretic study of glucose-6-phosphate dehydrogenase of HeLa and KB cell lines. Abstracts, Annual Meeting of the American Society for Human Genetics, p. 25.
Steele, M. W. (1969). Variation of glucose-6-phosphate dehydrogenase in the HeLa and Detroit 98 cell lines and their clonal derivatives. Biochem. Genet. 4 25.
Yoshida, A. (1966). Glucose-6-phosphate dehydrogenase of human erythrocytes I. Purification and characterization of normal (B+) enzyme. J. Biol. Chem. 241 4966.
Yoshida, A. (1967a). A single amino acid substitution (asparagine to aspartic acid) between normal (B+) and the common Negro variant (A+) of human glucose-6-phosphate dehydrogenase. Proc. Natl. Acad. Sci. 57 835.
Yoshida, A. (1967b). Human glucose-6-phosphate dehydrogenase: Purification and characterization of Negro type variant (A+) and comparison with normal enzyme (B+). Biochem. Genet. 1 81.
Yoshida, A. (1970). Enzyme purification by selective elution with substrate analog from ion-exchange columns: Application to glucose-6-phosphate dehydrogenase, pseudocholinesterase, lactate dehydrogenase, and alanine dehydrogenase. Anal. Biochem. 37 357.
Author information
Authors and Affiliations
Additional information
This research was supported by research grant GM 15253 from the National Institutes of Health.
Rights and permissions
About this article
Cite this article
Yoshida, A., Watanabe, S. & Gartler, S.M. Identification of HeLa cell glucose 6-phosphate dehydrogenase. Biochem Genet 5, 533–539 (1971). https://doi.org/10.1007/BF00485671
Received:
Revised:
Issue Date:
DOI: https://doi.org/10.1007/BF00485671