Zobrazeno 1 - 10
of 25
pro vyhledávání: '"William W. Farrar"'
Publikováno v:
Journal of Protein Chemistry. 18:103-115
Isoelectric focusing revealed three enolase isoforms in pig brain, which were designated as αα- (pI = 6.5), αγ- (pI = 5.6), and γγ-enolase (pI = 5.2). The pI of purified γγ-enolase was also 5.2. The γγ-enolase isoform of enolase was purifie
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c02cd0018ae03c8cc5d226d9f6da9310
https://doi.org/10.1023/a:1020659802760
https://doi.org/10.1023/a:1020659802760
Publikováno v:
Journal of Protein Chemistry. 17:855-866
Purified enolase from Bacillus subtilis has a native mass of approximately 370 kDa. Since B. subtilis enolase was found to have a subunit mass of 46.58 kDa, the quaternary structure of B. subtilis is octameric. The pl for B. subtilis enolase is 6.1,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b3443b7295bb5ff82f6a3bcae1935c83
https://doi.org/10.1023/a:1020790604887
https://doi.org/10.1023/a:1020790604887
Autor:
William W. Farrar, Gabert Farrar
Publikováno v:
The International Journal of Biochemistry & Cell Biology. 27:1145-1151
There are four pyruvate kinase isozymes in vertebrate tissues, designated as L, M1, M2, and R. Although pyruvate kinases have been purified and characterized from pig liver, muscle, kidney, and heart, the brain isozyme has not. The aim of this work w
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7feab8adbca3af312b3078e3009d8fe1
https://doi.org/10.1016/1357-2725(95)00090-c
https://doi.org/10.1016/1357-2725(95)00090-c
Publikováno v:
Journal of Protein Chemistry. 10:585-591
Using essentially a two-step procedure involving phosphocellulose column chromatography followed by gel filtration on Sephadex G200, pig heart pyruvate kinase (PH PyK) was purified 267-fold to at least 97% purity. PH PyK co-sedimented with rabbit mus
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::31a84632d9469258ce541c566eb95ed7
https://doi.org/10.1007/bf01025710
https://doi.org/10.1007/bf01025710
Autor:
William W. Farrar, William C. Deal
Publikováno v:
Journal of protein chemistry. 14(6)
Enolases (2-phospho-D-glycerate hydrolase, EC 4.2.1.11) were purified from both pig liver and muscle. Graphs of 1n C vs. r2 from sedimentation equilibrium experiments are linear, which suggests homogeneous preparations of liver and muscle enolases. F
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ce21592f0bc02aa7d2a6a32af6285e66
https://pubmed.ncbi.nlm.nih.gov/8593189
https://pubmed.ncbi.nlm.nih.gov/8593189
Autor:
Kent M. Plowman, William W. Farrar
Publikováno v:
International Journal of Biochemistry. 6:537-542
The initial velocity, product inhibition, and isotopic exchange data show that the substrates of bovine heart mitochondrial acetyl-CoA synthetase add to the enzyme in an ordered fashion, with MgATP adding first followed by the addition of acetate, th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::cc29a4429ea582080d615479722f2446
https://doi.org/10.1016/0020-711x(75)90069-5
https://doi.org/10.1016/0020-711x(75)90069-5
Autor:
William W. Farrar, Young Jo K. Farrar
Publikováno v:
International Journal of Biochemistry. 16:615-621
1. 1. Purification of heart (LDH-4) and flight muscle (LDH-2 and LDH-3) lactate dehydrogenase isoenzymes from the house sparrow. Passer domesticus, has been accomplished. 2. 2. Although these isoenzymes electrophoretically migrate reversed to most ot
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a7528267c26264385b5f2ceb2112bbc6
https://doi.org/10.1016/0020-711x(84)90030-2
https://doi.org/10.1016/0020-711x(84)90030-2
Autor:
William W. Farrar, Kent M. Plowman
Publikováno v:
International Journal of Biochemistry. 10:583-588
Product inhibition studies with bovine heart mitochondrial acetyl-CoA synthetase yielded the following results: 1. 1. Uncompetitive inhibition by AMP, and noncompetitive inhibition by acetyl-CoA as product inhibitors, both with CoA as the variable su
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1fa869fcb7660aa39ca4e41c49ca26f8
https://doi.org/10.1016/0020-711x(79)90019-3
https://doi.org/10.1016/0020-711x(79)90019-3
Publikováno v:
Comparative Biochemistry and Physiology Part B: Comparative Biochemistry. 75:317-321
1. 1. The isoelectric points (pI0), molecular weights and ammonium sulfate precipitation ranges for most of the glycolytic enzymes from house sparrow (Passer domesticus) flight muscle were determined. 2. 2. The pI0 for each enzyme is as follows: HK
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f1c0e6e3e7ecbacc8f5e4d1ad6b0e775
https://doi.org/10.1016/0305-0491(83)90332-2
https://doi.org/10.1016/0305-0491(83)90332-2
Autor:
William W. Farrar, Young Jo K. Farrar
Publikováno v:
Comparative biochemistry and physiology. B, Comparative biochemistry. 74(3)
1. 1. Study of the 11 glycolytic enzymes from the flight muscle of the house sparrow reveals an extreme range of activity levels. 2. 2. In order of ascending activity, the levels of these enzymes in Units per gram tissue are: HK ∗ (0.8 ± 0.2), GAP
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::786d61e10d4ecdd464c498a00d9ea89f
https://pubmed.ncbi.nlm.nih.gov/6839719
https://pubmed.ncbi.nlm.nih.gov/6839719