Zobrazeno 1 - 10
of 20
pro vyhledávání: '"W H, Strätling"'
Autor:
W H Strätling, B Ahne
Publikováno v:
Journal of Biological Chemistry. 269:17794-17801
Expression of the lysozyme gene in chicken macrophages is regulated by an enhancer located 2.7 kilobases upstream of the transcription start site. The organization of this enhancer was analyzed by in vitro assays (DNase I footprinting, dimethyl sulfa
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::8f56fe1825818b05f8839162bc536cc9
https://doi.org/10.1016/s0021-9258(17)32378-5
https://doi.org/10.1016/s0021-9258(17)32378-5
Publikováno v:
Journal of biomolecular NMR. 17(2)
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::01b7407f94cc9fada0243e73c7e16ba3
https://pubmed.ncbi.nlm.nih.gov/10921781
https://pubmed.ncbi.nlm.nih.gov/10921781
Autor:
B, Ahne, W H, Strätling
Publikováno v:
The Journal of biological chemistry. 269(27)
Expression of the lysozyme gene in chicken macrophages is regulated by an enhancer located 2.7 kilobases upstream of the transcription start site. The organization of this enhancer was analyzed by in vitro assays (DNase I footprinting, dimethyl sulfa
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::4eef7c7ce82f9aa3fea60cb65b591101
https://pubmed.ncbi.nlm.nih.gov/8027033
https://pubmed.ncbi.nlm.nih.gov/8027033
Publikováno v:
The Biochemical journal. 282
The structure of purified histone H5 in 1 M-NaClO4 and of H5 in nuclei was analysed by digestion with either one of three endoproteinases, papain, subtilisin or elastase, which preferentially cleave unstructured protein regions (and additionally with
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dcc65ad994dceff7269c1917d5e0e4b4
https://pubmed.ncbi.nlm.nih.gov/1546957
https://pubmed.ncbi.nlm.nih.gov/1546957
Publikováno v:
Nucleic Acids Research. 21:4408-4409
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f8b5fe07648db86dd6b1679f1cc4865d
https://doi.org/10.1093/nar/21.18.4408
https://doi.org/10.1093/nar/21.18.4408
Autor:
E Kotthaus, W H Strätling
Publikováno v:
Journal of Biological Chemistry. 259:13640-13643
Following treatment of hen erythrocyte nuclei with dimethyl 3,3'-dithiobispropionimidate, dimers between histones H1a, H1b, and H5 were extracted with 5% perchloric acid. They resolved electrophoretically into four sub-bands and these were identified
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::6f00ef5d94346789b5d5945b12ac6531
https://doi.org/10.1016/s0021-9258(18)89789-7
https://doi.org/10.1016/s0021-9258(18)89789-7
Publikováno v:
Biochemistry. 25:495-502
The chromatin structure encompassing the lysozyme gene domain in hen oviduct nuclei was studied by measuring the partitioning of coding and flanking sequences during chromatin fractionation and by analyzing the nucleosome repeat in response to microc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b3a64bf5f0e3b0136599d6b5ffd83ab0
https://doi.org/10.1021/bi00350a033
https://doi.org/10.1021/bi00350a033
Autor:
P V Loc, W H Strätling
Publikováno v:
The EMBO Journal. 7:655-664
The matrix attachment regions of the chicken lysozyme domain were studied in an in vitro DNA binding assay by incubating oviduct nuclear matrices with labeled restriction fragments. A strong attachment region was localized between 11.1 and 8.85 kb up
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1a12a6149b37ecfeb88bbdfb5d8bc6b4
https://doi.org/10.1002/j.1460-2075.1988.tb02860.x
https://doi.org/10.1002/j.1460-2075.1988.tb02860.x
Autor:
W H Strätling, E Kotthaus
Publikováno v:
Biochemical Journal. 224:1019-1022
We have studied the HClO4-solubility of histones H1 and H5 in hen erythrocyte nuclei after treatment with the cross-linker dimethyl 3,3′-dithiobispropionimidate (DTPI). The amount of acid-soluble, non-cross-linked, H1 and H5 histones was drasticall
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::42e60eae847f646f4d1e1a9965cca4d4
https://doi.org/10.1042/bj2241019
https://doi.org/10.1042/bj2241019
Publikováno v:
Journal of Biological Chemistry. 259:5893-5898
A rapid and reproducible method for the purification of the Ca/Mg-endonuclease from porcine and rat liver and for the stabilization of the enzyme activity is presented. The optimum conditions for enzyme activity were determined. The enzyme degrades d
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::363405650a9dbc437cdfcffe2d45a192
https://doi.org/10.1016/s0021-9258(18)91099-9
https://doi.org/10.1016/s0021-9258(18)91099-9