Zobrazeno 1 - 10
of 12
pro vyhledávání: '"D E Fahrney"'
Autor:
D E Fahrney, R J Seely
Publikováno v:
Journal of Biological Chemistry. 258:10835-10838
A phosphorus-containing metabolite that accounts for up to 80% of the total phosphate in perchloric acid extracts of Methanobacterium thermoautotrophicum ATCC 29183 was purified by chromatography on an anion exchange column. The proton-decoupled 31P
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::6a488cf877ca9ae3c57f5da658e33e75
https://doi.org/10.1016/s0021-9258(17)44350-x
https://doi.org/10.1016/s0021-9258(17)44350-x
Publikováno v:
Journal of Biological Chemistry. 253:6016-6020
The arginine deiminase (L-arginine iminohydrolase, EC 3.5.3.6) from Mycoplasma arthritidis catalyzes the irreversible hydrolysis of arginine and related guanidine derivatives to ammonia and the corresponding ureido analog of the substrate. The kineti
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::65f09efd35a0e029853261202b222f32
https://doi.org/10.1016/s0021-9258(17)34572-6
https://doi.org/10.1016/s0021-9258(17)34572-6
Publikováno v:
Journal of Biological Chemistry. 253:6010-6015
Hydrodynamic, chemical, and optical properties of arginine deiminase (EC 3.5.3.6) from Mycoplasma arthritidis are reported for the enzyme isolated from log phase cells. The S020,w and D020,w values of the enzyme are 5.48 S and 5.87 X 10(-7) cm3/s, re
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::07cd6e7074b7775d932b04764375b08c
https://doi.org/10.1016/s0021-9258(17)34571-4
https://doi.org/10.1016/s0021-9258(17)34571-4
Autor:
D E Fahrney, J L Weickmann
Publikováno v:
Journal of Biological Chemistry. 252:2615-2620
Arginine deiminase (EC 3.5.3.6) from Mycoplasma arthritidis ATCC 14152 has been purified 6-fold by a new procedure, protamine sulfate fractionation and DEAE-agarose chromatography. The yield was 75 to 85%. The homogeneity of the final preparation was
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0ad45e985a1f83c6c9643f2f7efc41de
https://doi.org/10.1016/s0021-9258(17)40503-5
https://doi.org/10.1016/s0021-9258(17)40503-5
Publikováno v:
Journal of Biological Chemistry. 261:11945-11948
The archaebacterium Methanobacterium thermoautotrophicum was grown at 65 degrees C in H2- and Pi-limited chemostat cultures at dilution rates corresponding to 3- and 4-h doubling times, respectively. Under these conditions the steady state concentrat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::fc44e4d5781c9bee975731a8c4ac23ef
https://doi.org/10.1016/s0021-9258(18)67184-4
https://doi.org/10.1016/s0021-9258(18)67184-4
Publikováno v:
The Journal of biological chemistry. 253(17)
The arginine deiminase (L-arginine iminohydrolase, EC 3.5.3.6) from Mycoplasma arthritidis catalyzes the irreversible hydrolysis of arginine and related guanidine derivatives to ammonia and the corresponding ureido analog of the substrate. The kineti
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::239cd48ebb9c99aff474603f924e2c4a
https://pubmed.ncbi.nlm.nih.gov/681336
https://pubmed.ncbi.nlm.nih.gov/681336
Publikováno v:
The Journal of biological chemistry. 261(26)
The archaebacterium Methanobacterium thermoautotrophicum was grown at 65 degrees C in H2- and Pi-limited chemostat cultures at dilution rates corresponding to 3- and 4-h doubling times, respectively. Under these conditions the steady state concentrat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::dba4f79dad8f5b16c30bfce0ebccff4e
https://pubmed.ncbi.nlm.nih.gov/3745174
https://pubmed.ncbi.nlm.nih.gov/3745174
Publikováno v:
Journal of bacteriology. 167(1)
The archaebacterium Methanobacterium thermoautotrophicum was grown in continuous culture at 65 degrees C in a phosphate-limited medium at specific growth rates from 0.06 to 0.28 h-1 (maximum growth rate [mu max] = 0.36 h-1). Cyclic-2,3-diphosphoglyce
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c89cf479c395a1d982967f7f974a5c26
https://pubmed.ncbi.nlm.nih.gov/3722128
https://pubmed.ncbi.nlm.nih.gov/3722128
Publikováno v:
The Journal of biological chemistry. 253(17)
Hydrodynamic, chemical, and optical properties of arginine deiminase (EC 3.5.3.6) from Mycoplasma arthritidis are reported for the enzyme isolated from log phase cells. The S020,w and D020,w values of the enzyme are 5.48 S and 5.87 X 10(-7) cm3/s, re
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::8e9e7fcb9e96170959389df0339a32ed
https://pubmed.ncbi.nlm.nih.gov/681335
https://pubmed.ncbi.nlm.nih.gov/681335
Autor:
J L, Weickmann, D E, Fahrney
Publikováno v:
The Journal of biological chemistry. 252(8)
Arginine deiminase (EC 3.5.3.6) from Mycoplasma arthritidis ATCC 14152 has been purified 6-fold by a new procedure, protamine sulfate fractionation and DEAE-agarose chromatography. The yield was 75 to 85%. The homogeneity of the final preparation was
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::d9ed0925aeb11bd901ce31d4498abe75
https://pubmed.ncbi.nlm.nih.gov/856796
https://pubmed.ncbi.nlm.nih.gov/856796