NATURAL CYTOTOXIC ANTIBODIES IN HUMAN BLOOD SERA WHICH REACT WITH MAMMALIAN CELLS AND BACTERIA: II. EFFECT OF HEATED HUMAN SERUM ON MICROORGANISMS

1963 ◽  
Vol 9 (2) ◽  
pp. 155-162 ◽  
Author(s):  
S. J. Webb ◽  
S. Fedoroff
Keyword(s):  
Escherichia Coli ◽  
Bacillus Subtilis ◽  
Human Serum ◽  
Human Blood ◽  
Mammalian Cells ◽  
Antibacterial Effect ◽  
Mycobacterium Phlei ◽  
Receptor Sites ◽  
Human Sera ◽  
Mouse Cells

It was found that certain bacterial and mammalian cells have similar receptor sites which react with natural antibodies present in human blood sera. Heated human sera which contain these antibodies are bacteriostatic to Escherichia coli and Mycobacterium phlei and bactericidal to Bacillus subtilis. This antibacterial effect is eliminated from heated human serum when the serum is treated with mouse cells.

scholarly journals Antibacterial activity of cis- and trans-resveratrol isolated from Polygonum cuspidatum rhizome

2006 ◽  
pp. 131-136 ◽  
Author(s):  
Zoran Kukric ◽  
Ljiljana Topalic-Trivunovic
Keyword(s):  
Escherichia Coli ◽  
Antimicrobial Activity ◽  
Antibacterial Activity ◽  
Bacillus Subtilis ◽  
Antibacterial Effect ◽  
Disk Diffusion ◽  
Diffusion Method ◽  
Polygonum Cuspidatum ◽  
Disk Diffusion Method ◽  
Cis And Trans

The work is concerned with the antibacterial effect of ethanolic solutions of cis- and trans-resveralrol (cis-.lrans-3,5.4'-trihydroxystilbene) obtained by the extraction (ethanol-water 1:1 v/v) of Polygonum cuspidatum rhizome. Antibacterial activity was tested by disk diffusion method on the following bacteria: Escherichia coli, Sarcina liitea. Bacillus subtilis and Staphylococcits sp., using extract concentrations of 5 mg/disk. All tests showed significant antimicrobial activity, whereby the extract with trans-resveratrol exhibited more significant effect than the extract of cis-resveratrol.

Characteristics and clinical application of a radiometric Escherichia coli-based phospholipase A2 assay modified for serum analysis

1993 ◽  
Vol 39 (4) ◽  
pp. 605-613 ◽  
Author(s):  
J Aufenanger ◽  
W Zimmer ◽  
R Kattermann
Keyword(s):  
Escherichia Coli ◽  
Fatty Acids ◽  
Oleic Acid ◽  
Phospholipase A2 ◽  
Human Serum ◽  
Solid Phase ◽  
Pla2 Activity ◽  
E Coli ◽  
Human Sera

Abstract Determination of activities of phospholipase A2 (PLA2) in human sera was based on the hydrolysis of phospholipids from [1-14C]oleic acid-labeled Escherichia coli biomembranes. The E. coli membranes served as substrate specifically for the PLA2 of human serum and were essentially resistant to other lipases in human sera, i.e., lipoprotein lipases, hepatic triacylglycerolipase, or pancreatic lipase in acute pancreatitis. Exchange of phospholipids between the serum and the biomembrane compartment aggravates the determination of PLA2 activity in human serum, which is naturally rich in phospholipids. In our modified E. coli assay, which overcomes these difficulties, the main substrate components phosphatidylethanolamine (70%) and cardiolipin (25%) were > 90% labeled in the sn-2 position. Fatty acids released by PLA2 activity were eluted from an aminopropyl solid-phase column directly into scintillation vials, where the radioactivity was counted. The ratio of [1-14C]oleic acid to released total fatty acids was used to calculate true enzymatic activity. The linear assay range extended from 0 to 3.6 U/L (0-60 nkat/L), with a detection limit of < 0.03 U/L (< 0.5 nkat/L). Within-assay imprecision (CV) was < 6% and between-assay is < 10% over the whole activity range. The normal range for men was 0-0.44 U/L (0-7.33 nkat/L) and for women 0.044-1.11 U/L (0.73-18.4 nkat/L). Patients with septicemia, pancreatitis, acute respiratory distress syndrome, or other severe diseases had PLA2 values up to 540 U/L (9000 nkat/L).

The Antibacterial Activity of the Extracts of Apocynum Venetum and Apocynum Venetum Fiber

2011 ◽  
Vol 233-235 ◽  
pp. 2328-2331 ◽  
Author(s):  
Hui Juan Wang ◽  
Hao Chen ◽  
Guang Ting Han
Keyword(s):  
Escherichia Coli ◽  
Staphylococcus Aureus ◽  
Antibacterial Activity ◽  
Bacillus Subtilis ◽  
Candida Albicans ◽  
Ethyl Acetate ◽  
Antibacterial Effect ◽  
Antibacterial Activities ◽  
Butyl Alcohol ◽  
Apocynum Venetum

In this study, the total flavone contents of Apocynum venetum extract and Apocynum venetum fiber extracts were evaluated. Their antibacterial activity was tested via testing the antibacterial effect of their aqueous, ethyl acetate and n-butyl alcohol extracts. The results were showed that both the materials extracts at the concentration of 100, 50mg/ml had significantly antibacterial activities against staphylococcus aureus, and had a few effect on bacillus subtilis, pseudomonadaceae, pseudomonas aeruginosa, staphylococcus epidermidis, escherichia coli and candida albicans.

scholarly journals Threonine synthesis from homoserine as a selectable marker in mammalian cells

1994 ◽  
Vol 299 (3) ◽  
pp. 637-644 ◽  
Author(s):  
W D Rees ◽  
S D Grant ◽  
S M Hay ◽  
K M Saqib
Keyword(s):  
Escherichia Coli ◽  
Active Region ◽  
Cell Lines ◽  
Hela Cells ◽  
Mammalian Cells ◽  
Selectable Marker ◽  
Threonine Synthase ◽  
Homoserine Kinase ◽  
Mouse Cells ◽  
High Concentrations

The plasmid pSVthrBC expresses the Escherichia coli thrB (homoserine kinase) and thrC (threonine synthase) genes in mouse cells and enables them to synthesize threonine from homoserine. After transfection with pSVthrBC and culture in medium containing homoserine, only cells that have incorporated pSVthrBC survive. Homoserine at concentrations greater than 1 mM is toxic to mammalian cells. Mouse cells selected from medium containing 5 mM homoserine had incorporated 20-100 copies of the plasmid per cell and had homoserine kinase activities of 0.001-0.012 nmol/min per mg of protein per copy. Cells selected from medium containing 10 mM homoserine had incorporated one or two copies of the plasmid per cell and had homoserine kinase activities of 0.06-0.39 nmol/min per mg of protein per copy. By using high concentrations of homoserine, it is possible to use pSVthrBC to select and isolate cell lines that have one or two copies of the plasmid incorporated into an active region of chromatin. CHO and HeLa cells have also been successfully transfected with pSVthrBC. COS-7 cells are naturally resistant to homoserine as they are able to metabolize homoserine.

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.

Human Blood Serum Rich in Factor V

1970 ◽  
Vol 24 (03/04) ◽  
pp. 334-337 ◽  
Author(s):  
R Honorato
Keyword(s):  
Blood Serum ◽  
Human Serum ◽  
Human Blood ◽  
Human Blood Serum ◽  
Factor V ◽  
The Stability

Summary1. A technique to obtain human serum rich in factor V is described.2. Calcium increases the stability of factor V in the serum.

STUDIES ON SULFATION FACTOR (SF) ACTIVITY OF HUMAN SERUM

1960 ◽  
Vol XXXV (III) ◽  
pp. 381-396 ◽  
Author(s):  
Sven Almqvist
Keyword(s):  
Human Serum ◽  
Normal Serum ◽  
Treatment Level ◽  
Response Curves ◽  
Normal Children ◽  
Significant Difference ◽  
Human Sera ◽  
Normal Humans ◽  
Pre Treatment ◽  
Dose Levels

ABSTRACT The sulfation factor (SF) activity of human sera has been estimated using a modification of the method of Daughaday et al. (1959). Each assay was statistically evaluated. The method had a mean precision of 0.14 and, used as an assay of GH of human serum, a sensitivity in three pituitary dwarfs of 0.1 to 0.6 μg of HGH/ml of serum. SF activity was found at all ages between 1 month and 75 years. There was a significantly lower mean SF activity below the age of half a year. Three cases of pituitary dwarfism had significantly low SF activities of sera. There was no significant difference between the SF activities of sera from untreated pituitary dwarfs and the sera from normal children below half a year of age. Dose-response curves with large volumes of sera from pituitary dwarfs and small volumes of sera from normal humans had the same slopes. Four mg of HGH prepared according to the method of Li & Papkoff (1956) resulted in a normal serum SF activity in each of the three dwarfs. A significant (P < 0.01) linear relationship was found between the concentration of SF activity of sera from these subjects and the logarithm of the dose of HGH given with dose levels of 1, 2 and 4 mg daily for three days. The decline of serum SF activity to the pre-treatment level following HGH in one dwarf suggested a half life not different from that indicated by others for growth hormone.

Antagonistic activity of Bacillus subtilis strains isolated from various sources

2018 ◽  
Vol 8 (2) ◽  
pp. 354-364
Author(s):  
A. N. Irkitova ◽  
A. V. Grebenshchikova ◽  
A. V. Matsyura
Keyword(s):  
Escherichia Coli ◽  
Bacillus Subtilis ◽  
Wild Strain ◽  
Fish Farming ◽  
Antagonistic Activity ◽  
Antagonistic Effect ◽  
E Coli ◽  
Long Period ◽  
Test Culture ◽  
Agar Media

<p>An important link in solving the problem of healthy food is the intensification of the livestock, poultry and fish farming, which is possible only in the adoption and rigorous implementation of the concept of rational feeding of animals. In the implementation of this concept required is the application of probiotic preparations. Currently, there is an increased interest in spore probiotics. In many ways, this can be explained by the fact that they use no vegetative forms of the bacilli and their spores. This property provides spore probiotics a number of advantages: they are not whimsical, easily could be selected, cultivated, and dried. Moreover, they are resistant to various factors and could remain viable during a long period. One of the most famous spore microorganisms, which are widely used in agriculture, is <em>Bacillus subtilis</em>. Among the requirements imposed to probiotic microorganisms is mandatory – antagonistic activity to pathogenic and conditional-pathogenic microflora. The article presents the results of the analysis of antagonistic activity of collection strains of <em>B. subtilis</em>, and strains isolated from commercial preparations. We studied the antagonistic activity on agar and liquid nutrient medias to trigger different antagonism mechanisms of <em>B. subtilis</em>. On agar media, we applied three diffusion methods: perpendicular bands, agar blocks, agar wells. We also applied the method of co-incubating the test culture (<em>Escherichia coli</em>) and the antagonist (or its supernatant) in the nutrient broth. Our results demonstrated that all our explored strains of <em>B. subtilis</em> have antimicrobial activity against a wild strain of <em>E. coli</em>, but to varying degrees. We identified strains of <em>B. subtilis</em> with the highest antagonistic effect that can be recommended for inclusion in microbial preparations for agriculture.</p><p><em><br /></em><em></em></p>

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