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Proc Natl Acad Sci U S A ; 69(1): 69-73, 1972 Jan.
Article in English | MEDLINE | ID: mdl-4500556

ABSTRACT

Man-mouse and man-Syrian hamster somatic hybrid cell lines were prepared by fusion of mouse A9 or hamster TG2 cells, which are deficient in hypoxanthine-guanine phosphoribosyl transferase, with cells of a diploid fibroblastic strain, KOP-1, derived from a woman heterozygous for an X-autosome translocation. 61 clones were derived in nonselective medium and 85 sublines of these were derived in selective media: 53 in hypoxanthine-aminopterine-thymidine and 32 in 8-azaguanine. All three human X-linked markers studied, i.e., hypoxanthineguanine phosphoribosyl transferase (EC 2.4.2.8), glucose-6-phosphate dehydrogenase (EC 1.1.1.49), and phosphoglycerate kinase (EC 2.7.2.3), were present together, or absent together, in most of these clones and sublines. However, loss or retention of only phosphoglycerate kinase was occasionally observed, even in the absence of selective growth, while no evidence of separation of hypoxanthine-guanine phosphoribosyl transferase from glucose-6-phosphate dehydrogenase occurred. Cytological examination of eight man-hamster clonal lines by the quinacrine fluorescent technique showed that human phosphoglycerate kinase was only present when the translocation chromosome carrying most of the long arm of the X chromosome was present. The presence of human glucose-6-phosphate dehydrogenase and hypoxanthine-guanine phosphoribosyl transferase was not related to the presence or absence of this chromosome, but appeared to be correlated with the presence of the other translocation chromosome.


Subject(s)
Chromosome Mapping , Hybrid Cells , Sex Chromosomes , Animals , Cell Fusion , Cell Line , Chromosome Aberrations , Clone Cells , Cricetinae , Culture Media , Female , Genetic Linkage , Glucosephosphate Dehydrogenase/metabolism , Humans , Inosine Nucleotides , Karyotyping , Mice , Mitosis , Pentosephosphates , Pentosyltransferases/metabolism , Phosphoglycerate Kinase/metabolism , Sex Chromosomes/enzymology
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