THE EFFECT OF DIHYDROSTREPTOMYCIN ON THE FORMATION OF ADAPTIVE ENZYMES BY A STRAIN OF ESCHERICHIA COLI

1955 ◽  
Vol 33 (1) ◽  
pp. 792-796
Author(s):  
Susan M. Roote ◽  
W. J. Polglase
Keyword(s):  
Escherichia Coli ◽  
Glucuronic Acid ◽  
E Coli ◽  
Enzyme Formation

The adaptive formation of enzymes for the oxidation of L-arabinose, lactose, and D-glucuronic acid was inhibited by dihydrostreptomycin in a strain of Escherichia coli which would not grow in the presence of this antibiotic. Adaptive enzyme formation was not inhibited in E. coli variants which would grow in the presence of dihydrostreptomycin or which required the antibiotic for growth.

THE EFFECT OF DIHYDROSTREPTOMYCIN ON THE FORMATION OF ADAPTIVE ENZYMES BY A STRAIN OF ESCHERICHIA COLI

1955 ◽  
Vol 33 (5) ◽  
pp. 792-796 ◽  
Author(s):  
Susan M. Roote ◽  
W. J. Polglase
Keyword(s):  
Escherichia Coli ◽  
Glucuronic Acid ◽  
E Coli ◽  
Enzyme Formation

The adaptive formation of enzymes for the oxidation of L-arabinose, lactose, and D-glucuronic acid was inhibited by dihydrostreptomycin in a strain of Escherichia coli which would not grow in the presence of this antibiotic. Adaptive enzyme formation was not inhibited in E. coli variants which would grow in the presence of dihydrostreptomycin or which required the antibiotic for growth.

ADAPTIVE ENZYME FORMATION BY DIHYDROSTREPTOMYCIN- DEPENDENT ESCHERICHIA COLI

1956 ◽  
Vol 34 (3) ◽  
pp. 558-562 ◽  
Author(s):  
W. J. Polglase ◽  
Susan Peretz ◽  
Susan M. Roote
Keyword(s):  
Escherichia Coli ◽  
Cell Multiplication ◽  
E Coli ◽  
Enzyme Formation

An apparent requirement for dihydrostreptomycin for the formation of adaptive enzymes has been demonstrated in a strain of E. coli which requires this antibiotic for cell multiplication. The effect of dihydrostreptomycin on the formation of adaptive enzymes by E. coli has been shown to be consistent with the effect of the antibiotic on bacterial multiplication.

Behavior of Hemorrhagic Escherichia coli O157:H7 During the Manufacture of Cottage Cheese

1992 ◽  
Vol 55 (5) ◽  
pp. 379-381 ◽  
Author(s):  
MARLENE M. AROCHA ◽  
MELINDA MCVEY ◽  
SUSAN D. LODER ◽  
JOHN H. RUPNOW ◽  
LLOYD BULLERMAN
Keyword(s):  
Escherichia Coli ◽  
Glucuronic Acid ◽  
Skim Milk ◽  
Enterohemorrhagic Escherichia Coli ◽  
Cottage Cheese ◽  
Escherichia Coli O157 ◽  
Phenol Red ◽  
E Coli ◽  
Heat Treated ◽  
And Control

The ability of enterohemorrhagic Escherichia coli O157:H7 to grow and survive during the manufacture of Cottage cheese was determined. Pasteurized skim milk artificially contaminated with E. coli O157:H7 was used to make Cottage cheese by the washed curd method. E. coli O157:H7 was enumerated by surface plating samples on MacConkey sorbitol agar with 5-bromo-4-chloro-3-indoxyl-β-D-glucuronic acid cyclohexylammonium salt (MSA-BCIG) and incubating at 42°C for 24 h. The heat treated samples were previously inoculated into a modified EC broth with novobiocin and incubated static at 35°C for 24 h. Sorbitol and β-glucuronidase negative colonies were picked from MSA-BCIG, spread on Levine eosin methylene blue agar plates and phenol red sorbitol agar plates with 4-methylumbelliferyl-β-D-glucuronide (PRS-MUG) added for confirmation. E. coli O157:H7 increased 100-fold in numbers during the manufacturing process, but death occurred during cooking of the curd and whey. The pH and acidity did not halt the growth of this pathogen during the manufacture of the cheese; furthermore, the values of these parameters were the same between the contaminated and control samples.

scholarly journals Microbial metabolism of amino alcohols. Formation of coenzyme B12-dependent ethanolamine ammonia-lyase and its concerted induction in Escherichia coli

1978 ◽  
Vol 176 (3) ◽  
pp. 751-757 ◽  
Author(s):  
C M Blackwell ◽  
J M Turner
Keyword(s):  
Escherichia Coli ◽  
Enzyme Stability ◽  
Kinetic Studies ◽  
Coenzyme B12 ◽  
E Coli ◽  
Immunological Tests ◽  
Enzyme Formation ◽  
Acting In Concert

1. Kinetic studies of ethanolamine ammonia-lyase formation by Escherichia coli suggested that coenzyme B12 (5′-deoxyadenosylcobalamin), with ethanolamine, is a co-inducer. 2. Enzymic and immunological tests failed to show the formation of complementary enzyme components induced separately by ethanolamine and cobalamin respectively. 3. Although specific for ethanolamine as the substrate, enzyme formation was induced by certain analogues, e.g. 2-aminopropan-1-ol. 4. Experiments with cyano[57Co]-cobalamin suggested that neither coenzyme B12 nor some more tightly bound coenzymically inactive cobamide was necessary for enzyme stability in vitro. 5. Mutants of E. coli were obtained which formed ethanolamine ammonia-lyase apoenzyme constitutively, showing that neither ethanolamine nor cobalamin was required for assembly or post-transcriptional stability of the enzyme in vivo. Constitutive enzyme formation was subject to catabolite repression, particularly by glucose. 6. It appears likely that ethanolamine and coenzyme B12, acting in concert, induce ethanolamine ammonia-lyase formation. The term ‘concerted’ induction is proposed for this phenomenon.

THE EFFECT OF DIHYDROSTREPTOMYCIN ON THE FORMATION OF BETA-GALACTOSIDASE BY ESCHERICHIA COLI

1956 ◽  
Vol 34 (1) ◽  
pp. 554-557 ◽  
Author(s):  
W. J. Polglase
Keyword(s):  
Escherichia Coli ◽  
E Coli ◽  
Enzyme Formation ◽  
Beta Galactosidase

In confirmation and extension of previous observations on the effect of dihydrostreptomycin on adaptive enzyme formation, it was observed that the formation of the enzyme β-galactosidase was inhibited by dihydrostreptomycin in a strain of Escherichia coli which could not multiply in the presence of this antibiotic. Formation of β-galactosidase was not inhibited in E. coli variants which could multiply in the presence of dihydrostreptomycin or which required the antibiotic for multiplication.

THE EFFECT OF DIHYDROSTREPTOMYCIN ON THE FORMATION OF BETA-GALACTOSIDASE BY ESCHERICHIA COLI

1956 ◽  
Vol 34 (3) ◽  
pp. 554-557 ◽  
Author(s):  
W. J. Polglase
Keyword(s):  
Escherichia Coli ◽  
E Coli ◽  
Enzyme Formation ◽  
Beta Galactosidase

In confirmation and extension of previous observations on the effect of dihydrostreptomycin on adaptive enzyme formation, it was observed that the formation of the enzyme β-galactosidase was inhibited by dihydrostreptomycin in a strain of Escherichia coli which could not multiply in the presence of this antibiotic. Formation of β-galactosidase was not inhibited in E. coli variants which could multiply in the presence of dihydrostreptomycin or which required the antibiotic for multiplication.

ADAPTIVE ENZYME FORMATION BY DIHYDROSTREPTOMYCIN- DEPENDENT ESCHERICHIA COLI

1956 ◽  
Vol 34 (1) ◽  
pp. 558-562
Author(s):  
W. J. Polglase ◽  
Susan Peretz ◽  
Susan M. Roote
Keyword(s):  
Escherichia Coli ◽  
Cell Multiplication ◽  
E Coli ◽  
Enzyme Formation

An apparent requirement for dihydrostreptomycin for the formation of adaptive enzymes has been demonstrated in a strain of E. coli which requires this antibiotic for cell multiplication. The effect of dihydrostreptomycin on the formation of adaptive enzymes by E. coli has been shown to be consistent with the effect of the antibiotic on bacterial multiplication.

Sites of Adsorption of the Bacteriophages T3 and T5 on the Wall of Escherichia Coli B.

1967 ◽  
Vol 25 ◽  
pp. 96-97
Author(s):  
Manfred E. Bayer
Keyword(s):  
Escherichia Coli ◽  
Cell Wall ◽  
Electron Microscope ◽  
Uranyl Acetate ◽  
E Coli ◽  
Receptor Sites ◽  
Rigid Cell Wall ◽  
Host Cell Surface ◽  
Bacterial Viruses ◽  
Escherichia Coli B

Bacterial viruses adsorb specifically to receptors on the host cell surface. Although the chemical composition of some of the cell wall receptors for bacteriophages of the T-series has been described and the number of receptor sites has been estimated to be 150 to 300 per E. coli cell, the localization of the sites on the bacterial wall has been unknown.When logarithmically growing cells of E. coli are transferred into a medium containing 20% sucrose, the cells plasmolize: the protoplast shrinks and becomes separated from the somewhat rigid cell wall. When these cells are fixed in 8% Formaldehyde, post-fixed in OsO4/uranyl acetate, embedded in Vestopal W, then cut in an ultramicrotome and observed with the electron microscope, the separation of protoplast and wall becomes clearly visible, (Fig. 1, 2). At a number of locations however, the protoplasmic membrane adheres to the wall even under the considerable pull of the shrinking protoplast. Thus numerous connecting bridges are maintained between protoplast and cell wall. Estimations of the total number of such wall/membrane associations yield a number of about 300 per cell.

The Influence of Glycosylation on the Catalytic and Fibrinolytic Properties of Pro-Urokinase

1992 ◽  
Vol 68 (05) ◽  
pp. 539-544 ◽  
Author(s):  
Catherine Lenich ◽  
Ralph Pannell ◽  
Jack Henkin ◽  
Victor Gurewich
Keyword(s):  
Escherichia Coli ◽  
Mammalian Cell ◽  
Human Gene ◽  
Culture Media ◽  
Mammalian Cell Culture ◽  
Glycosylation Site ◽  
Clot Lysis ◽  
Cell Culture Media ◽  
E Coli ◽  
The Uk

SummaryWe previously found that human pro-UK expressed in Escherichia coli is more active in fibrinolysis than recombinant human pro-UK obtained from mammalian cell culture media. To determine whether this difference is related to the lack of glycosylation of the E. coli product, we compared the activity of E. coli-derived pro-UK [(-)pro-UK] with that of a glycosylated pro-UK [(+)pro-UK] and of a mutant of pro-UK missing the glycosylation site at Asn-302 [(-) (302) pro-UK]. The latter two pro-UKs were obtained by expression of the human gene in a mammalian cell. The nonglycosylated pro-UKs were activated by plasmin more efficiently (≈2-fold) and were more active in clot lysis (1.5-fold) than the (+)pro-UK. Similarly, the nonglycosylated two-chain derivatives (UKs) were more active against plasminogen and were more rapidly inactivated by plasma inhibitors than the (+)UK.These findings indicate that glycosylation at Asn-302 influences the activity of pro-UK/UK and could be the major factor responsible for the enhanced activity of E. coli-derived pro-UK.

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