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Thursday, July 16, 2020 | History

2 edition of Permeability barrier to galactosides in escherichia coli. found in the catalog.

Permeability barrier to galactosides in escherichia coli.

Fred M. Kahan

Permeability barrier to galactosides in escherichia coli.

by Fred M. Kahan

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Published .
Written in English


Edition Notes

Thesis (M.A.) -- University of Toronto, 1959.

The Physical Object
Pagination1 v.
ID Numbers
Open LibraryOL20497649M

The effects of organic pesticides on inner membrane permeability in Escherichia coli ML35 Article (PDF Available) in Cell Biology and Toxicology 21(2) April with Reads. Sigma-Aldrich offers a number of β-Galactosidase from Escherichia coli products. View information & documentation regarding β-Galactosidase from Escherichia coli, including CAS, MSDS & more.

Abstract. The effects of N,N′-dicyclohexylcarbodiimide (DCCD) on the growth of Streptococcus faecalis, and on the growth, β-galactosidase synthesis, and various membrane-mediated processes, were studied in wild-type Escherichia coli JE and its lipopolysaccharide-defective mutant NS1. DCCD ( mM) completely inhibited the growth of S. faecalis and E. coli NS1 but had little effect on. Since strains of Escherichia coli K12 bearing deletions of the lac Z gene have a very small residual activity toward ONPG, there must also be a second β-galactosidase in E. coli.

The β-galactosidase activity in the E. coli cells coexpressing TF-PR D30N and β-Gal PR was ± μmol/min/mg of total proteins, which was higher than the β-galactosidase activity ( ± μmol/min/mg of total proteins) detected in the presence of the wild-type HIV protease. This indicated that the D30N HIV protease mutant. Abstract. The steroidal diamine irehdiamine A (IDA) is a potent inhibitor of bacteriophage growth and macromolecular synthesis in Escherichia using radioactive 42 K and 14 C-thiomethylgalactoside (TMG), rapid effects of IDA and related steroids, both on the influx of potassium and TMG via their respective transport systems and on the efflux (leakage) of radioactivity from the treated.


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Permeability barrier to galactosides in escherichia coli by Fred M. Kahan Download PDF EPUB FB2

Investigation of the β-galactosidase activity of Escherichia coli B has confirmed the view that the access of β-galactosides to the intracellular site of enzyme activity is limited by a permeability barrier.

Evidence presented indicates that passage of β-galactosides across this barrier is effected by the combined action of a process of physical diffusion and that of an enzyme-like transport by: 6. Can J Biochem Physiol. Jan; A study of the permeability barrier to beta-galactosides in Escherichia coli B.

HOLMES R, SHEININ R, CROCKER by: 6. A STUDY OF THE PERMEABILITY BARRIER TO β-GALACTOSIDES IN ESCHERICHIA COLI B. Canadian Journal of Biochemistry and Physiology39 (1), DOI: /o DOI: /o Rose Sheinin, Bruce F. by:   A study of the permeability barrier to beta-galactosides in Escherichia coli B.

A study of the permeability barrier to beta-galactosides in Escherichia coli B. HOLMES R, SHEININ R, CROCKER BF. Canadian Journal of Biochemistry and Physiology, 01 Jan45 Cited by: 6. Sampson, B. A., Misra, R. & Benson, S. Identification and characterization of a new gene of Escherichia coli K involved in outer membrane permeability.

GeneticsCited by:   The effects of antimicrobial peptide F1on the release of cytoplasmic β-galactosidase in the Escherichia coli cells. Generally, the cytoplasmic β-galactosidase cannot pass through the integrated inner membrane of E. coli, but it can be detected extracellularly if the.

One set in the status with IPTG (5mM) and another set in the status of adding H2O as the control experiment. 15 labeled microfuge tubing which contain Aµl of the CTAB solution which used to kills the E.

coli cells and lyses the cells to let go of the contents including I. -galactosidase were prepared and placed in the ice bath. ml of. Abstract. A mutant ofEscherichia coli sensitive to proteinase (MP2) has been isolated and characterized briefly.

MP2 cells were impaired by Pronase, showing a decrease of the cell turbidity both in growing cell and in cell suspension, while the parental cells remained unimpaired.

Basic Lab Skills: β-Galactosidase Induction in Escherichia coli. Safety Tip of the Day: Don't touch the E. coli and don't breathe the chloroform!. Summary. The lac operon is a segment of DNA in the bacteria \(E. coli \) consisting of 4 adjacent genes that are controlled together.

In the presence of lactose, the operon is turned ON and enables the bacteria to let lactose into the cell and. action of EDTA in E.

coli: the increased permeability to exter- nally supplied small molecules. The parameters of EDTA treatment resulting in this permeability change, and the mecha- nism whereby treated cells repair their permeability barrier, will be explored.

The results suggest that. Rapid killing of Escherichia coli by intact or disrupted rabbit granulocytes or by granulocyte fractions was found to be accompanied by an equally rapid increase in permeability of the envelope.

This increase in permeability was detected by determining entry of substances that normally do not. Toxicity of selenite to Escherichia coli ML is enhanced if the organism is inoculated into a selenite medium which contains lactose as the only carbon source.

In media of this type, the cells must synthesize β-galactosidase before growth can take place, and a lag period is produced which is proportional to the selenite concentration. ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS() The Effects of Selenite on ß-Galactosidase Induction in Escherichia coli J.

SCALA,1 P. ULBRICH,2 AND H. WILLIAMS From the Department of Biochemistry, Savage Hall, Cornell University, Ithaca, New York Received Janu Toxicity of selenite to Escherichia coli ML is enhanced if the organism is inocu- lated into a.

the time and pH of preincubation of BPI with E. coli: e.g., for E. coli J5 treated with human BPI, t1/2 = 79 min at pH and 10 min at pH The serum albumin effects on BPI action are the same in wild-type E.

coli and in a mutant strain lacking an activatable phospholipase, indicating that serum albumin does not act by sequestering membrane. The outer membrane of Gram-negative bacteria presents a formidable barrier to the discovery of new antibiotics needed to combat infections by multidrug-resistant bacteria.

Targeting essential proteins or processes directly exposed to the environment could bypass this obstacle. Here, we describe a monoclonal antibody that selectively and potently antagonizes BamA, which folds and.

Glycinin basic peptide (GBP) exhibited strong antibacterial activities against Escherichia coli (E. coli). Atomic force microscopy (AFM) revealed GBP could destroy E. coli cells, to lead to eventually cell death.

The increase of leakage of Ca 2 +, K +, and Mg 2 + of E. coli cells suggested GBP treatment resulted in the damage to E.

coli cells. The increase of permeability of outer membrane. The ebg beta-galactosidase of Escherichia coli K strain LC has been purified and characterized. Strain LC is a Lac+ revertant of a mutant with a deletion of the lacZ beta-galactosidase gene.

Its new ebg beta-galactosidase activity was shown to be due to a discrete protein, immunologically unrelated to lacZ beta-galactosidase. Its kinetics of action conformed to those of a simple.

a study of the permeability barrier to β-galactosides in escherichia coli b. holmes, rose sheinin, bruce f. crocker the induced concurrent formation of α-galactosidase and β-galactosidase in escherichia coli b. rose sheinin. At cooling rates greater than °C/min, the survival became dependent on subsequent warming bility damage, as measured by release of UV-absorbing material, potassium and β-galactosidase, and increased accessibility of glucosephosphate dehydrogenase to its substrates, was dependent on the cooling rate when cells were frozen in either water or saline.

The intake of certain nutrients, including ferric ion, is facilitated by the outer membrane-localized transporters. Due to ferric insolubility at physiological pH, Escherichia coli secretes a chelator, enterobactin, outside the cell and then transports back the enterobactin-ferric complex via an outer membrane receptor protein, FepA, whose activity is dependent on the proton motive force.

The parameters involved in the action of β-galactosidase (EC ) (Escherichia coli) on allolactose, the natural inducer of lac operon inwere low allolactose concentrations only galactose and glucose were formed, while at high allolactose concentrations transgalactolytic oligosaccharides were also produced.CAPTURE OF GLYCEROL BY CELLS OF ESCHERICHIA COLI.

Biochim Biophys Acta. Mar 29; – Hayashi SI, Lin EC. Product induction of glycerol kinase in Escherichia coli. J Mol Biol. Dec; 14 (2)– HOLMES R, SHEININ R, CROCKER BF. A study of the permeability barrier to beta-galactosides in Escherichia coli B.

Escherichia coli is the most widely studied and frequently used host for recombinant protein production because its genetics are well-characterized, the culture periods are short, and protein production levels are high [1,2,3].Because E.

coli has both inner and outer membranes, recombinant proteins produced in this host can localize to the cytoplasm, the periplasm, or the culture medium [2, 4].