Zobrazeno 1 - 10
of 10
pro vyhledávání: '"S. H. G. Allen"'
Publikováno v:
Journal of bacteriology. 175(22)
The Bacillus subtilis gene encoding acetate kinase was identified on the basis of sequence similarity to the Escherichia coli ackA gene and to a second E. coli gene closely related to ackA. Insertional inactivation of this region of the B. subtilis c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5860e10d2fbf7ce8a424a1a7fdc35ccf
https://pubmed.ncbi.nlm.nih.gov/8226682
https://pubmed.ncbi.nlm.nih.gov/8226682
Publikováno v:
Journal of Biological Chemistry. 238:1637-1642
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0ad434e9fd9c1dd8761d9174182caed0
https://doi.org/10.1016/s0021-9258(18)81114-0
https://doi.org/10.1016/s0021-9258(18)81114-0
Publikováno v:
Journal of Bacteriology. 87:171-187
Allen , S. H. G. (Western Reserve University, Cleveland, Ohio), R. W. Kellermeyer, R. L. Stjernholm, and Harland G. Wood . Purification and properties of enzymes involved in the propionic acid fermentation. J. Bacteriol. 87: 171–187. 1964.—Chroma
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::30b31e974a7615b8a625f35a69118d76
https://doi.org/10.1128/jb.87.1.171-187.1964
https://doi.org/10.1128/jb.87.1.171-187.1964
Autor:
Dorothy M. Powelson, S. H. G. Allen
Publikováno v:
Journal of Bacteriology. 75:184-189
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d22e3e9982882aa2a3fc996d6eb0a044
https://doi.org/10.1128/jb.75.2.184-189.1958
https://doi.org/10.1128/jb.75.2.184-189.1958
Publikováno v:
Journal of Biological Chemistry. 238:PC2889-PC2892
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::bb423d2bc0d9941717c0984d67b0c943
https://doi.org/10.1016/s0021-9258(18)67915-3
https://doi.org/10.1016/s0021-9258(18)67915-3
Publikováno v:
Journal of Biological Chemistry. 238:547-556
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d9fb0332372c82cf933dde99b6110e80
https://doi.org/10.1016/s0021-9258(18)81297-2
https://doi.org/10.1016/s0021-9258(18)81297-2
Publikováno v:
Journal of Biological Chemistry. 239:2562-2569
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f2f54fe52789b8669d5c3f52f8f2af17
https://doi.org/10.1016/s0021-9258(18)93888-3
https://doi.org/10.1016/s0021-9258(18)93888-3
Publisher Summary This chapter describes the enzyme that is prepared from Propionibacterium shermanii (52W). The (S)-methyhnalonyl-CoA formed as a result of racemase action is converted to propionyl-CoA and oxaloacetate through the oxaloacetate trans
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https://explore.openaire.eu/search/publication?articleId=doi_________::7fae485a77b05b51e0376acec22ceb87
https://doi.org/10.1016/0076-6879(69)13038-4
https://doi.org/10.1016/0076-6879(69)13038-4
Publikováno v:
Archives of biochemistry and biophysics. 105
Propionyl-CoA carboxylase containing tritium-labeled biotin has been partially purified from Mycobacterium smegmatis. After preliminary purification the purity of the enzyme can be followed by specific radioactivity. The propionyl-CoA carboxylase of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0e789f033216bc9fb402e90fc815fc24
https://pubmed.ncbi.nlm.nih.gov/14236632
https://pubmed.ncbi.nlm.nih.gov/14236632
Publikováno v:
Annals of the New York Academy of Sciences. 112
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5b751a8016d1562b7e8ad79832f78f90
https://pubmed.ncbi.nlm.nih.gov/14167300
https://pubmed.ncbi.nlm.nih.gov/14167300