Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Carol A. Blyth"'
Autor:
Carol A. Blyth, Jeremy R. Knowles
Publikováno v:
Journal of the American Chemical Society. 93:3017-3021
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::2adea3f0c266d96648fdd01ee70e84df
https://doi.org/10.1021/ja00741a033
https://doi.org/10.1021/ja00741a033
Autor:
Carol A. Blyth, Jeremy R. Knowles
Publikováno v:
Journal of the American Chemical Society. 93:3021-3027
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0090cc88b2ac440af84d8393200abd7e
https://doi.org/10.1021/ja00741a034
https://doi.org/10.1021/ja00741a034
Autor:
Carol A. Blyth, Robert B. Freedman, David Ridge, Brian R. Rabin, Jane Hammond, Rosemary P. Clark, Jill Vinter, Derrick W. James, David L. Williams
Publikováno v:
European Journal of Biochemistry. 32:57-62
1 The binding curves of oestradiol and testosterone to plasma membranes from male or female rat livers show no specific sites of high affinity. 2 Plasma membranes from male and female rat livers show no disulphide interchange activity. It is conclude
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f42657e2dd8dc7b2f7ebf653c7b977c0
https://doi.org/10.1111/j.1432-1033.1973.tb02578.x
https://doi.org/10.1111/j.1432-1033.1973.tb02578.x
Publikováno v:
European journal of biochemistry. 29(2)
1 Smooth reticular membranes from male rat liver contain high affinity binding sites for oestradiol. Similar membranes from females contain analogous sites for testosterone. 2 Rough membranes from which polysomes have been removed by EDTA (degranulat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::86ab68a4d72b3bb400c7f17f44f49d35
https://pubmed.ncbi.nlm.nih.gov/4343090
https://pubmed.ncbi.nlm.nih.gov/4343090
Publikováno v:
European journal of biochemistry. 20(4)
1 A new method is described for the titration of membranes with steroid hormones, and the binding curves for male and female smooth rat liver microsomes with oestradiol and testosterone are reported. 2 At least three classes of binding site exist, in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bbfd77a91402c3f54d658e3f6dc5d4cd
https://pubmed.ncbi.nlm.nih.gov/5087619
https://pubmed.ncbi.nlm.nih.gov/5087619
Publikováno v:
Nature: New biology. 230(13)
Direct studies of the binding of oestradiol and testosterone to male and female membranes in vitro show that there are sex specific binding sites which have a high affinity for steroid hormones.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0be3bc01062620baa55ffb96d05d4e7b
https://pubmed.ncbi.nlm.nih.gov/5279466
https://pubmed.ncbi.nlm.nih.gov/5279466
Autor:
Brian R. Rabin, Delma Doherty, David J. Williams, Carol A. Blyth, Anne Roobol, R. B. Freedman, G. H. Sunshine
Publikováno v:
Effects of Drugs on Cellular Control Mechanisms ISBN: 9781349013234
Protein synthesis in the cell, involves particulate elements called ribosomes which translate the information coded as specific nucleotide sequences in messenger RNA molecules into amino-acid sequences of proteins [1]. Ribosomes are frequently found
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a75f3afbc2bcbeadc2b2e712f038e376
https://doi.org/10.1007/978-1-349-01321-0_3
https://doi.org/10.1007/978-1-349-01321-0_3
Reticular membranes contain an enzyme which catalyses the rearrangement of disulphide bonds in proteins. The enzyme is present in both rough and smooth membranes, but is inactive in the rough membranes unless the polysomes are removed. If polysomes a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::43325cd8e5a62ac0f051c54aa341bad3
https://doi.org/10.1016/b978-0-12-761250-8.50010-0
https://doi.org/10.1016/b978-0-12-761250-8.50010-0
Autor:
Carol A. Blyth, Jeremy R. Knowles
Publikováno v:
Chemischer Informationsdienst. Organische Chemie. 2
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::517ec6ca89f5bec666ec7b9135b64c2c
https://doi.org/10.1002/chin.197136191
https://doi.org/10.1002/chin.197136191