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Your search keyword '"Frischauf, Anne-Marie"' showing total 8 results
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8 results on '"Frischauf, Anne-Marie"'

2. Mapping of cosmid clones in Huntington's disease region of chromosome 4

Author

Whaley, William L., Bates, Gillian P., Novelletto, Andrea, Sedlacek, Z., Cheng, Shirley, Romano, Donna, Ormondroyd, Elizabeth, Allitto, Bernice, Lin, Carol, Youngman, Sandra, Baxendale, Sarah, Bucan, Maja, Altherr, Michael, Wasmuth, John, Wexler, Nancy S., Frontali, Marina, Frischauf, Anne-Marie, Lehrach, Hans, MacDonald, Marcy E., and Gusella, James F.

Published
1991
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5. Covalent Attachment of DNA to Agarose.

Author

Arndt-Jovin, Donna J., Jovin, Thomas M., Bähr, Wolfgang, Frischauf, Anne-Marie, and Marquardt, Maria

Subjects
SEPHAROSE, AFFINITY chromatography, ENZYMES, DNA, OLIGONUCLEOTIDES, DNA-binding proteins
Abstract

DNA has been covalently linked to insoluble matrices of agarose (Sepharose) in high yield using cyanogen bromide activation. Both double-stranded and single-stranded DNA have been coupled with yields up to 225 µmol/mg dry weight Sepharose or 3-8 μmol nucleotide phosphate/ml bed volume. The DNA-Sepharose has been used for (a) the affinity chromatography of various enzymes (Escherichia coli DNA polymerase I and RNA polymerase) from crude extracts or after initial purification steps, resulting in high yields and degrees of purification, and for (b) nucleic add hybridization. The DNA-Sepharose is stable W high temperature, prolonged storage, and in the case of single-stranded DNA, can be washed with NaOH to destroy nuclease activity and to release any digested oligonucleotides or mononucleotides. [ABSTRACT FROM AUTHOR]

Published
1975
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7. Nucleotide sequence of cDNA coding for Semliki Forest virus membrane glycoproteins

Author

Garoff, Henrik, Frischauf, Anne-Marie, Simons, Kai, Lehrach, Hans, and Delius, Hajo

Abstract

The genes coding for the three membrane polypeptides of Semliki Forest virus have been sequenced and the primary structures of the proteins deduced. The amino acid sequence gives further insight into how the transmembrane structure of the three-chain virus membrane glycoprotein is generated in the infected cell.

Published
1980
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8. Huntington disease-linked locusD4S111 exposed as the α-<span style="font-variant:small-caps">l</span> -iduronidase gene

Author

MacDonald, Marcy, Scott, Hamish, Whaley, William, Pohl, Thomas, Wasmuth, John, Lehrach, Hans, Morris, C., Frischauf, Anne-Marie, Hopwood, John, and Gusella, James

Abstract

Abstract: agr-l-Iduronidase (IDUA) has been intensively studied due to its causative role in mucopolysaccharidosis type I (Hurler, Scheie and Hurler/Scheie syndromes). The recent cloning of a human IDUA cDNA has resulted in a reevaluation of the chromosomal location of this gene. Previously assigned to chromosome 22, IDUA now has been localized to 4p16.3, the region of chromosome 4 associated with Huntington's disease (HD). The existence of a battery of cloned DNA, physical map information, and genetic polymorphism data for this region has allowed the rapid fine mapping of IDUA within the terminal cytogenetic band of 4p. IDUA was found to be coincident with D4S111, an anonymous locus displaying a highly informative multiallele DNA polymorphism. This map location, 1.1×106 bp from the telomere, makes IDUA the most distal cloned gene assigned to 4p. However, it falls within a segment of 4p16.3 that has been eliminated from the HD candidate region, excluding a role for IDUA in this disorder.

Published
1991
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