Abstract
The mouse X-linkedPgk-1 gene encodes phosphoglycerate kinase. When transfected into human cells, thePgk-1b allele causes the appearance of mouse PGK-1b enzyme activity. We describe here cloning of mousePgk-1a, an allele ofPgk-1 which encodes an enzyme, PGK-1a, with distinct electrophoretic mobility. We constructed recombinants between the DNA encodingPgk-1b andPgk-1a and transfected these constructs into human to assess the electrophoretic characteristics of each recombinant. In this way the charge variation between the two proteins was localized to exons 4 or 5. Sequencing of these exons revealed a single base-pair difference between the two alleles at codon 155, which predicts the amino acids lysine and threonine in PGK-1b and PGK-1a, respectively. A number of other DNA sequence polymorphisms exist betweenPgk-1b andPgk-1a including part of an L1 repeated element unique toPgk-1a.
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This work was supported by the Medical Research Council of Canada, the National Cancer Institute of Canada, and the Deutsche Forschungsgemeinschaft, SFB 304.
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Boer, P.H., Potten, H., Adra, C.N. et al. Polymorphisms in the coding and noncoding regions of murinePgk-1 alleles. Biochem Genet 28, 299–308 (1990). https://doi.org/10.1007/BF02401419
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DOI: https://doi.org/10.1007/BF02401419