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Janice Y. Chou Bruce D. Weintraub Saul W. Rosen Jacqueline Whangpeng Howard D. Sussman Joan R. Haughom J. C. Robinson 《In vitro cellular & developmental biology. Plant》1976,12(8):589-594
Summary Several cell lines, originally thought to be derived from a human placenta at term but possibly HeLa-contaminated, have been
studied. These cells secrete a protein indistinguishable immunochemically from the alpha subunit of chorionic gonadotropin
but not the beta subunit of chorionic gonadotropin or placental lactogen. Complete chorionic gonadotropin was detected but
amounted to less than 1% of the level of the alpha subunit. The cells also produce an alkaline phosphatase similar to placental
alkaline phosphatase in immunochemical, gel-electrophoretic, and heat-denaturation properties. They induce tumor growth when
inoculated into nude mice. These cells are aneuploid and have a model chromosome number of 66. The common HeLa karyologic
markers, designated 1, 2, and 3, and A-type glucose-6-phosphate dehydrogenase are present in these cells. HeLa cells have
not previously been shown to secrete theα subunit of hCG. 相似文献
146.
Elizabeth J. McCosh Donald L. Meyer Jacqueline Dupont 《Prostaglandins & other lipid mediators》1976,12(4):471-486
A radioimmunoassay procedure for the determination of PGE1, PGE2, and PGF2α is presented. The procedure involves the pre-precipitation of each prostaglandin specific antiserum with the precipitating antisera (ARGG), and the use of these antisera mixtures in assaying for PGE1, PGE2, and PGF2α. Applicability of the methods to unextracted plasma, serum and myocardial homogenate has been demonstrated through tests of specificity, recovery, reproducability and parallelism. A mathematical correction for cross-reactivity between PGE1 and PGE2, and their opposing antisera is given. To demonstrate the utility of the methodology in differentiation of experimental variables, prostaglandin concentrations in unincubated serum, incubated serum, and the rate of prostaglandin production in serum of dogs are given. 相似文献
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Jacqueline Jollés FranÇOise Schoentgen Pierre Jollès Ellen M. Prager Allan C. Wilson 《Journal of molecular evolution》1976,8(1):59-78
Summary The amino acid sequence of lysozyme c from chachalaca egg white was determined. Like other bird lysozymes c, that of the chachalaca has 129 amino acid residues. It differs from other avian lysozymes c by 27 to 31 amino acid substitutions as well as by being devoid of phenylalanine. It contains substitutions at 9 positions which are invariant in the other 7 bird lysozymes of known sequence. Although the chachalaca is classified zoologically in the order Galliformes, which includes chickens and other pheasant-like birds, its lysozyme differs more from those of pheasant-like birds than do the lysozymes c of ducks. Phylogenetic analysis of the sequence comparisons confirms that the lineage leading to chachalaca lysozyme c separated from that leading to other galliform lysozymes c before the duck lysozyme c lineage did. This indicates a contrast between protein evolution and evolution at the organismal level. Immunological comparison of chachalacalysozyme c with other lysozymes of known sequence provides further support for the proposal that immunological cross-reactivity is strongly dependent on degree of sequence resemblance among bird lysozymes.103rd communication on lysozymes from the Laboratory of P. Jollès. Supported in part by grants from C.N.R.S. (ER 102), I.N.S.E.R.M. (Groupe de recherche U-116), N.S.F. (GB-42028X), and N.I.H. (GM-21509). 相似文献
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Jacqueline Verdière Eric Petrochilo 《Biochemical and biophysical research communications》1975,67(4):1451-1458
Mutations specific for iso-2 cytochrome c were obtained in strains bearing a deletion of the structural gene of iso-1-cytochrome c. In this genetic context the mutations entail an inability to grow on glycerol. One of these mutants was shown to have a modified iso-2-cytochrome c as witnessed by its lack of stability and modified chromatographic behaviour. Genetic studies showed the mutations to be allelic to the mutation cyp3-15 previously identified by Clavilier (1) as a specific enhancer of iso-2-cytochrome c synthesis. The simplesthypothesis to explain the results is that the CYP3 locus is the structural gene for iso-2-cytochrome c. 相似文献
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