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  • American Society for Microbiology  (20)
  • Russell, J B  (20)
  • 1990-1994  (20)
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  • American Society for Microbiology  (20)
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Language
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  • 1990-1994  (20)
Year
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Subjects(RVK)
  • 1
    Online Resource
    Online Resource
    Cloning and sequencing of a Bacteroides ruminicola B(1)4 endoglucanase gene
    American Society for Microbiology ; 1990
    In:  Journal of Bacteriology Vol. 172, No. 7 ( 1990-07), p. 3620-3630
    Details
    In: Journal of Bacteriology, American Society for Microbiology, Vol. 172, No. 7 ( 1990-07), p. 3620-3630
    Abstract: Bacteroides ruminicola B(1)4, a noncellulolytic rumen bacterium, produces an endoglucanase (carboxymethylcellulase [CMCase]) that is excreted into the culture supernatant. Cultures grown on glucose, fructose, maltose, mannose, and cellobiose had high specific activities of CMCase (greater than 3 mmol of reducing sugar per mg of protein per min), but its synthesis was repressed by sucrose. B. rumincola did not grow on either ball-milled or acid-swollen cellulose even though the CMCase could hydrolyze swollen cellulose. The CMCase gene was cloned into Escherichia coli, and its nucleotide sequence contained a single open reading frame coding for a protein of 40,481 daltons. The enzyme was overproduced in E. coli under the control of the tac promoter and purified to homogeneity. The N-terminal sequence, amino acid composition, and molecular weight of the purified enzyme were similar to the values predicted from the open reading frame of the DNA sequence. However, the CMCase present in B. ruminicola was found to have a monomer molecular weight of 88,000 by Western immunoblotting. This discrepancy appeared to have resulted from our having cloned only part of the CMCase gene into E. coli. The amino acid sequence of the CMCase showed homology to sequences of beta-glucanases from Ruminococcus albus and Clostridium thermocellum.
    Type of Medium: Online Resource
    ISSN: 0021-9193 , 1098-5530
    URL: Article
    DOI: 10.1128/jb.172.7.3620-3630.1990
    Language: English
    Publisher: American Society for Microbiology
    Publication Date: 1990
    detail.hit.zdb_id: 1481988-0
    SSG: 12
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  • 2
    Online Resource
    Online Resource
    Electrogenic glutamine uptake by Peptostreptococcus anaerobius and generation of a transmembrane potential
    American Society for Microbiology ; 1994
    In:  Journal of Bacteriology Vol. 176, No. 5 ( 1994-03), p. 1303-1308
    Details
    In: Journal of Bacteriology, American Society for Microbiology, Vol. 176, No. 5 ( 1994-03), p. 1303-1308
    Abstract: Peptostreptococcus anaerobius converted glutamine stoichiometrically to ammonia and pyroglutamic acid, and the Eadie-Hofstee plot of glutamine transport was biphasic. High-affinity, sodium-dependent glutamine transport (affinity constant [Kt] of 1.5 microM) could be driven by the chemical gradient of sodium, and more than 20 mM sodium was required for half-maximal velocity. High-affinity glutamine transport was not stimulated or inhibited by a membrane potential (delta psi). Low-affinity glutamine transport had a rate which was directly proportional to the external glutamine concentration, required less than 100 microM sodium, and was inhibited strongly by a delta psi. Cells which were treated with N,N-dicyclohexylcarbodiimide to inhibit the F1F0 ATPase still generated a delta psi but did so only if the external glutamine concentration was greater than 15 mM. Low-affinity glutamine uptake could not be saturated by as much as 200 mM glutamine, but glutamine-1 accounts for only a small fraction of the total glutamine at physiological pH values (pH 6 to 7). On the basis of these results, it appeared that the low-affinity glutamine transport was an electrogenic mechanism which was converting a chemical gradient of glutamine-1 into a delta psi. Other mechanisms of delta psi generation (electrogenic glutamine-pyroglutamate or -ammonium exchange) could not be demonstrated.
    Type of Medium: Online Resource
    ISSN: 0021-9193 , 1098-5530
    URL: Article
    DOI: 10.1128/jb.176.5.1303-1308.1994
    Language: English
    Publisher: American Society for Microbiology
    Publication Date: 1994
    detail.hit.zdb_id: 1481988-0
    SSG: 12
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  • 3
    Online Resource
    Online Resource
    Electrogenic L-malate transport by Lactobacillus plantarum: a basis for energy derivation from malolactic fermentation
    American Society for Microbiology ; 1991
    In:  Journal of Bacteriology Vol. 173, No. 19 ( 1991-10), p. 6199-6206
    Details
    In: Journal of Bacteriology, American Society for Microbiology, Vol. 173, No. 19 ( 1991-10), p. 6199-6206
    Abstract: L-Malate transport in Lactobacillus plantarum was inducible, and the pH optimum was 4.5. Malate uptake could be driven by an artificial proton gradient (delta pH) or an electroneutral lactate efflux. Because L-lactate efflux was unable to drive L-malate transport in the absence of a delta pH, it did not appear that the carrier was a malate-lactate exchanger. The kinetics of malate transport were, however, biphasic, suggesting that the external malate concentration was also serving as a driving force for low-affinity malate uptake. Because the electrical potential (delta psi, inside negative) inhibited malate transport, it appeared that the malate transport-lactate efflux couple was electrogenic (net negative) at high concentrations of malate. De-energized cells that were provided with malate only generated a large proton motive force (greater than 100 mV) when the malate concentration was greater than 5 mM, and malate only caused an increase in cell yield (glucose-limited chemostats) when malate accumulated in the culture vessel. The use of the malate gradient to drive malate transport (facilitated diffusion) explains how L. plantarum derives energy from malolactic fermentation, a process which does not involve substrate-level phosphorylation.
    Type of Medium: Online Resource
    ISSN: 0021-9193 , 1098-5530
    URL: Article
    DOI: 10.1128/jb.173.19.6199-6206.1991
    Language: English
    Publisher: American Society for Microbiology
    Publication Date: 1991
    detail.hit.zdb_id: 1481988-0
    SSG: 12
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  • 4
    Online Resource
    Online Resource
    A Bacteroides ruminicola 1,4-beta-D-endoglucanase is encoded in two reading frames
    American Society for Microbiology ; 1991
    In:  Journal of Bacteriology Vol. 173, No. 21 ( 1991-11), p. 6919-6926
    Details
    In: Journal of Bacteriology, American Society for Microbiology, Vol. 173, No. 21 ( 1991-11), p. 6919-6926
    Abstract: Escherichia coli transformed with a plasmid containing a Bacteroides ruminicola endoglucanase (carboxymethyl cellulase [CMCase]) gene produced three immunologically cross-reacting CMCases which had molecular weights of 40,500, 84,000, and 88,000, while B. ruminicola produced CMCases with molecular weights of 82,000 and 88,000. The two B. ruminicola enzymes (purified from culture supernatants) had different N-terminal amino acid sequences, but each enzyme was encoded by the same gene (three independent clones had the same DNA sequence). The 88,000-molecular-weight CMCase (88K CMCase) gene appeared to contain two open reading frames which overlapped for 18 bp and were -1 out of frame, and each open reading frame contained several stop codons near the overlap region. The two 88K CMCase open reading frames had enough DNA to produce a protein of 106K, but the mobility of the enzyme in sodium dodecyl sulfate gels gave a value which was 20% lower. On the basis of the -1 frame shift and the large deviation in theoretical versus actual size, it appears that an unusual event (e.g., ribosomal hopping or RNA splicing) is involved in either the translation or the transcription of the 88K B. ruminicola CMCase gene. The 82K CMCase was completely encoded in the second reading frame, and its size was in agreement with the DNA sequence.
    Type of Medium: Online Resource
    ISSN: 0021-9193 , 1098-5530
    URL: Article
    DOI: 10.1128/jb.173.21.6919-6926.1991
    Language: English
    Publisher: American Society for Microbiology
    Publication Date: 1991
    detail.hit.zdb_id: 1481988-0
    SSG: 12
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  • 5
    Online Resource
    Online Resource
    Properties of a genetically reconstructed Prevotella ruminicola endoglucanase
    American Society for Microbiology ; 1992
    In:  Applied and Environmental Microbiology Vol. 58, No. 11 ( 1992-11), p. 3593-3597
    Details
    In: Applied and Environmental Microbiology, American Society for Microbiology, Vol. 58, No. 11 ( 1992-11), p. 3593-3597
    Abstract: A pUC19-derived plasmid was constructed that coded for a hybrid cellulase with the Thermomonospora fusca E2 cellulose-binding domain at its C terminus joined to the Prevotella ruminicola 40.5-kDa carboxymethyl cellulase (CMCase). The hybrid enzyme was purified and characterized enzymatically. It bound tightly to cellulose, and its specific activities on carboxymethyl cellulose, amorphous cellulose, and ball-milled cellulose were 1.5, 10, and 8 times that of the 40.5-kDa CMCase, respectively. Furthermore, the modified enzyme gave synergism with an exocellulase in the degradation of filter paper, while the 40.5-kDa CMCase did not.
    Type of Medium: Online Resource
    ISSN: 0099-2240 , 1098-5336
    URL: Article
    DOI: 10.1128/aem.58.11.3593-3597.1992
    RVK:
    WA 15000
    Language: English
    Publisher: American Society for Microbiology
    Publication Date: 1992
    detail.hit.zdb_id: 223011-2
    detail.hit.zdb_id: 1478346-0
    SSG: 12
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  • 6
    Online Resource
    Online Resource
    Resistance of proline-containing peptides to ruminal degradation in vitro
    American Society for Microbiology ; 1992
    In:  Applied and Environmental Microbiology Vol. 58, No. 12 ( 1992-12), p. 3954-3958
    Details
    In: Applied and Environmental Microbiology, American Society for Microbiology, Vol. 58, No. 12 ( 1992-12), p. 3954-3958
    Abstract: Mixed ruminal bacteria utilized an enzymatic digest of casein at a rate faster than that for an enzymatic digest of gelatin, but neither amino acid source was completely utilized even when the incubation period was as long as 96 h. Since the reaction of ninhydrin with the residual nonammonia, nonprotein nitrogen was more than twofold stronger when the samples were hydrolyzed with 6 N HCl, it appeared that much of the residual nitrogen was from peptides. Approximately 66% of the nonammonia, nonprotein, ninhydrin-reactive material could not be recovered as amino acids, but there was a significant decrease in total amino acid nitrogen when the samples were pretreated with a C18 Sep-Pak column to remove peptides. The resistant peptides had an abundance of proline, and subsequent incubations showed that synthetic dipeptides which contained proline were hydrolyzed slowly. Lysine appears to be the amino acid which is most apt to limit ruminant production. Dipeptides containing proline and lysine were hydrolyzed at least fivefold slower than lysine-alanine. Methionine, another potentially limiting amino acid, was also degraded at a slower (2.5-fold) rate when it was present as part of a proline dipeptide.
    Type of Medium: Online Resource
    ISSN: 0099-2240 , 1098-5336
    URL: Article
    DOI: 10.1128/aem.58.12.3954-3958.1992
    RVK:
    WA 15000
    Language: English
    Publisher: American Society for Microbiology
    Publication Date: 1992
    detail.hit.zdb_id: 223011-2
    detail.hit.zdb_id: 1478346-0
    SSG: 12
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  • 7
    Online Resource
    Online Resource
    Low-affinity, high-capacity system of glucose transport in the ruminal bacterium Streptococcus bovis: evidence for a mechanism of facilitated diffusion
    American Society for Microbiology ; 1990
    In:  Applied and Environmental Microbiology Vol. 56, No. 11 ( 1990-11), p. 3304-3307
    Details
    In: Applied and Environmental Microbiology, American Society for Microbiology, Vol. 56, No. 11 ( 1990-11), p. 3304-3307
    Abstract: The glucose phosphotransferase system (PTS) of Streptococcus bovis could not account for the glucose consumption of exponential cultures, and the kinetics of glucose transport were biphasic. A PTS-deficient mutant lost the high-affinity, low-capacity system but retained its ability to take up glucose at high substrate concentrations. The low-affinity, high-capacity system did not require a proton motive force or ATP and could not be driven by an artificial membrane potential in the presence or absence of sodium. Since low-affinity transport was directly proportional to the external substrate concentration and exhibited counterflow kinetics, it appeared that a facilitated-diffusion mechanism was responsible for glucose transport at high substrate concentrations.
    Type of Medium: Online Resource
    ISSN: 0099-2240 , 1098-5336
    URL: Article
    DOI: 10.1128/aem.56.11.3304-3307.1990
    RVK:
    WA 15000
    Language: English
    Publisher: American Society for Microbiology
    Publication Date: 1990
    detail.hit.zdb_id: 223011-2
    detail.hit.zdb_id: 1478346-0
    SSG: 12
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  • 8
    Online Resource
    Online Resource
    Energy-spilling reactions of Streptococcus bovis and resistance of its membrane to proton conductance
    American Society for Microbiology ; 1994
    In:  Applied and Environmental Microbiology Vol. 60, No. 6 ( 1994-06), p. 1942-1948
    Details
    In: Applied and Environmental Microbiology, American Society for Microbiology, Vol. 60, No. 6 ( 1994-06), p. 1942-1948
    Abstract: Glucose-excess cultures of Streptococcus bovis consumed glucose faster than the amount that could be explained by growth or maintenance, and nongrowing chloramphenicol-treated cells had a rate of glucose consumption that was 10-fold greater than the maintenance rate. Because N,N-dicyclohexylcarbodiimide, an inhibitor of the membrane-bound F1F0 ATPase, eliminated the nongrowth energy dissipation (energy spilling) without a decrease in ATP and the rate of energy spilling could be increased by the protonophore 3,3',4',5-tetrachlorosalicylanilide, it appeared that a futile cycle of protons through the cell membrane was responsible for most of the energy spilling. When the rate of energy spilling was decreased gradually with iodoacetate, there was only a small decrease in the phosphorylation potential (delta G'p) and the theoretical estimate of H+ per ATP decreased from 4.2 to 3.6. On the bases of this ratio of H+ to ATP and the rate of ATP production, the flux of protons (amperage) across the cell membrane was directly proportional to the rate of energy spilling. Amperage values estimated from delta G'p were, however, nearly twice as great as values which were estimated from the heat production (delta H) of the cells [amperage = (0.38 x wattage)/delta p]. The last comparison indicated that only a fraction of the delta G of ATP hydrolysis was harvested by the F1F0 ATPase to pump protons. Both estimates of amperage indicated that the resistance of the cell membrane to proton conductance was inversely proportional to the log of the energy-spilling rate.
    Type of Medium: Online Resource
    ISSN: 0099-2240 , 1098-5336
    URL: Article
    DOI: 10.1128/aem.60.6.1942-1948.1994
    RVK:
    WA 15000
    Language: English
    Publisher: American Society for Microbiology
    Publication Date: 1994
    detail.hit.zdb_id: 223011-2
    detail.hit.zdb_id: 1478346-0
    SSG: 12
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  • 9
    Online Resource
    Online Resource
    Energetics of arginine and lysine transport by whole cells and membrane vesicles of strain SR, a monensin-sensitive ruminal bacterium
    American Society for Microbiology ; 1992
    In:  Applied and Environmental Microbiology Vol. 58, No. 3 ( 1992-03), p. 969-975
    Details
    In: Applied and Environmental Microbiology, American Society for Microbiology, Vol. 58, No. 3 ( 1992-03), p. 969-975
    Abstract: Strain SR, a monensin-sensitive, ammonia-producing ruminal bacterium, grew rapidly on arginine and lysine, but only if sodium was present. Arginine transport could be driven by either an electrical potential or a chemical gradient of sodium. Arginine was converted to ornithine, and it appeared that ornithine efflux created a sodium gradient which in turn drove arginine transport. There was a linear decline in arginine transport as pH was decreased from 7.5 to 5.5, and the cells did not grow at a pH less than 6.0. The Eadie-Hofstee plot was biphasic, and arginine could also be taken by a high-capacity diffusion mechanism. Because arginine was a strong inhibitor of lysine transport and lysine was a weak inhibitor of arginine transport, it appeared that both lysine and arginine were taken up by an arginine-lysine carrier which had a preference for arginine. The rate of lysine fermentation was always proportional to the extracellular lysine concentration, and facilitated diffusion was the dominant mechanism of lysine transport. When SR was grown in continuous culture on arginine or lysine, the theoretical maximal growth yield was similar (13 g of cells per mol of ATP), but the apparent maintenance energy requirement for arginine was greater than lysine (9.4 versus 4.4 mmol of ATP per g of cells per h). On the basis of differences in yield and maintenance energy, it appeared that active arginine transport accounted for approximately 40% of the total ATP.
    Type of Medium: Online Resource
    ISSN: 0099-2240 , 1098-5336
    URL: Article
    DOI: 10.1128/aem.58.3.969-975.1992
    RVK:
    WA 15000
    Language: English
    Publisher: American Society for Microbiology
    Publication Date: 1992
    detail.hit.zdb_id: 223011-2
    detail.hit.zdb_id: 1478346-0
    SSG: 12
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  • 10
    Online Resource
    Online Resource
    Effect of monensin on the specific activity of ammonia production by ruminal bacteria and disappearance of amino nitrogen from the rumen
    American Society for Microbiology ; 1993
    In:  Applied and Environmental Microbiology Vol. 59, No. 10 ( 1993-10), p. 3250-3254
    Details
    In: Applied and Environmental Microbiology, American Society for Microbiology, Vol. 59, No. 10 ( 1993-10), p. 3250-3254
    Abstract: When unadapted mixed ruminal bacteria (312 mg of protein per liter) were treated with monensin (5 mM) in vitro, the rates of ammonia production from enzymatic digests of casein, gelatin, and soy protein (0.5 g of N per liter) were decreased from 46 +/- 2 to 24 +/- 1, 20 +/- 1 to 7 +/- 1, and 40 +/- 2 to 18 +/- 2 nmol/mg of protein per min, respectively. Monensin also caused a decrease in ammonia production in vivo. Nonlactating dairy cows which were fed 0.56 kg of timothy hay 12 times per day had a steady-state ruminal ammonia concentration of 2.7 +/- 0.1 mM, and the ammonia concentration decreased to 1.2 +/- 0.2 mM when monensin (350 mg/day) was added to the diet. The decrease in ammonia production was associated with a 10-fold reduction (4.1 x 10(6) versus 4.2 x 10(5)/ml) in the most probable number of ammonia-producing ruminal bacteria that could use protein hydrolysate as an energy source. Monensin had little effect on the most probable number of carbohydrate-utilizing ruminal bacteria (6.5 versus 7.0 x 10(8)/ml). The addition of protein hydrolysates (560 g) to the rumen caused a rapid increase in the ammonia concentration, but this increase was at least 30% lower when the animals were fed monensin.(ABSTRACT TRUNCATED AT 250 WORDS)
    Type of Medium: Online Resource
    ISSN: 0099-2240 , 1098-5336
    URL: Article
    DOI: 10.1128/aem.59.10.3250-3254.1993
    RVK:
    WA 15000
    Language: English
    Publisher: American Society for Microbiology
    Publication Date: 1993
    detail.hit.zdb_id: 223011-2
    detail.hit.zdb_id: 1478346-0
    SSG: 12
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