The Cloning, Isolation and Characterization of a Biologically Active Human Enzyme, Urokinase, in E. Coli

1984 ◽  
pp. 281-293 ◽  
Author(s):  
P. P. Hung
Keyword(s):  
Biologically Active ◽  
E Coli ◽  
Isolation And Characterization ◽  
Human Enzyme

scholarly journals Isolation and characterization of escherichia coli in ready-to-eat foods vended in Islamic University, Kushtia

1970 ◽  
Vol 18 ◽  
pp. 99-103 ◽  
Author(s):  
S Biswas ◽  
MAK Parvez ◽  
M Shafiquzzaman ◽  
S Nahar ◽  
MN Rahman
Keyword(s):  
Escherichia Coli ◽  
Pattern Analysis ◽  
University Campus ◽  
Rflp Pattern ◽  
E Coli ◽  
Fish Meat ◽  
Isolation And Characterization ◽  
Food Borne ◽  
Identification And Characterization

Context: Escherichia coli is shed in the feces of warm blooded animals and humans and thus potential for public health. Detection and characterization of E. coli in the ready-to-eat (RTE) foods concerns due to their presence indicates fecal contamination of the food.   Objective: To identify, characterize and RFLP pattern analysis of E. coli isolated from RTE foods vended in Islamic University campus, Kushtia.   Materials and Methods: Fifty samples from four types of consumed foods in six student halls of residence, some temporary restaurants of Islamic University, Kushtia were assessed for bacterial contamination by standard methods. Identification and characterization of E. coli isolates were performed using IMViC tests. Genomic DNA was used to perform RFLP pattern analysis.   Results: Thirty seven out of 50 (74%) examined samples of RTE foods had E. coli contamination. The highest number of E. coli was isolated from vegetable oriented RTE foods (90.90%) and fish, meat and cereals samples were also significantly E. coli positive. RFLP profiling of two E. coli isolates were observed.   Conclusion: The results of this study provide evidence that some RTE foods had unsatisfactory levels of contamination with E. coli. Thus street vended RTE food could be important potential vehicles for food-borne diseases. Molecular characterization may be exploited to identify food borne pathogen among different species.  Keywords: Ready-to-eat foods; Escherichia coli; RFLP pattern DOI: http://dx.doi.org/10.3329/jbs.v18i0.8783 JBS 2010; 18(0): 99-103

scholarly journals Isolation and characterization of bacteria residing in the oral, gut, and fecal samples of different pheasant species

2023 ◽  
Vol 83 ◽  
Author(s):  
M. Mushtaq ◽  
S. M. Bukhari ◽  
S. Ahmad ◽  
A. Khattak ◽  
M. B. Chattha ◽  
...  
Keyword(s):  
Bacterial Species ◽  
Gut Contents ◽  
Phasianus Colchicus ◽  
Gut Content ◽  
E Coli ◽  
Colony Forming Unit ◽  
Isolation And Characterization ◽  
Staphylococcus Spp ◽  
Campylobacter Spp

Abstract There is a paucity of research conducted on microbial prevalence in pheasants. The microbiota of captive birds has zoonotic significance and must be characterize. Present study is therefore planned to assess the microbiota from oral, fecal and gut content of captive avian species. It will be helpful in characterization of harmful microbes. Different samples taken from oral, gut and feces of ring-necked pheasants (Phasianus colchicus), green pheasants (Phasianus versicolor), golden pheasant (Chrysolophus pictus) and silver pheasant (Lophura nycthemera). Samples were collected, diluted, and inoculated onto different agar plates (MacConkey, SS agar, MSA and nutrient agar) for cultivation of bacterial species. Colonies of E.coli, Staphylococcus spp. Brachyspira spp. and Campylobacter spp were observed based on colony morphology. Colony forming unit showed E. coli as frequently found bacteria in fecal, oral and gut contents of all the above pheasants. The overall significance difference was found among bacterial species of golden pheasants, green pheasant, ring-necked pheasant, and silver pheasants. It was concluded that E.coli is predominant isolated from heathy pheasants followed by Campylobacter, Staphylococcus and Brachyspira.

Isolation and Characterization of Levoglucosan Metabolizing Bacteria

2021 ◽  
Author(s):  
Ajay S. Arya ◽  
Minh T. H. Hang ◽  
Mark A. Eiteman
Keyword(s):  
Recombinant Expression ◽  
Bacterial Species ◽  
Soluble Carbohydrate ◽  
Rrna Gene ◽  
Gene Products ◽  
16S Rrna Gene Sequences ◽  
E Coli ◽  
Isolation And Characterization ◽  
Charred Wood

Bacteria were isolated from wastewater and soil containing charred wood remnants based on their ability to use levoglucosan as a sole carbon source and on their levoglucosan dehydrogenase (LGDH) activity. On the basis of their 16S rRNA gene sequences, these bacteria represented diverse genera of Microbacterium, Paenibacillus , Shinella , and Klebsiella . Genomic sequencing of the isolates verified that two isolates represented novel species, Paenibacillus athensensis MEC069 T and Shinella sumterensis MEC087 T , while the remaining isolates were closely related to either Microbacterium lacusdiani or Klebsiella pneumoniae . The genetic sequence of LGDH, lgdA , was found in the genomes of these four isolates as well as Pseudarthrobacter phenanthrenivorans Sphe3. The identity of the P. phenanthrenivorans LGDH was experimentally verified following recombinant expression in E. coli . Comparison of the putative genes surrounding lgdA in the isolate genomes indicated that several other gene products facilitate the bacterial catabolism of levoglucosan, including a putative sugar isomerase and several transport proteins. Importance Levoglucosan is the most prevalent soluble carbohydrate remaining after high temperature pyrolysis of lignocellulosic biomass, but it is not fermented by typical production microbes such as Escherichia coli and Saccharomyces cerevisiae . A few fungi metabolize levoglucosan via the enzyme levoglucosan kinase, while several bacteria metabolize levoglucosan via levoglucosan dehydrogenase. This study describes the isolation and characterization of four bacterial species which degrade levoglucosan. Each isolate is shown to contain several genes within an operon involved in levoglucosan degradation, furthering our understanding of bacteria which metabolize levoglucosan.

Cloning and expression of DiT33 from Dirofilaria immitis: a specific and early marker of heartworm infection

Parasitology ◽  
1996 ◽  
Vol 112 (3) ◽  
pp. 331-338 ◽  
Author(s):  
X. Q. Hong ◽  
J. Santiago Mejia ◽  
S. Kumar ◽  
F. B. Perler ◽  
C. K. S. Carlow
Keyword(s):  
Dirofilaria Immitis ◽  
Cloning And Expression ◽  
E Coli ◽  
Spliced Leader ◽  
Isolation And Characterization ◽  
The Family ◽  
Heartworm Infection ◽  
High Level ◽  
Control And Management

SUMMARYDirofilaria immitis is an important filarial parasite of dogs and cats, and a useful model for human filariasis. Current diagnostic tests for heartworm infection in animals rely on the presence of fecund female worms (usually found 6·5 months post-infection or later) and therefore fail to detect pre-patent infections. Putative pepsin inhibitors from 2 filarial parasites of humans namely Onchocerca volvulus (Ov33, Oc3.6, OvDSB) and Brugia malayi (Bm33), have been shown to be useful in diagnosis of onchocerciasis and lymphatic filariasis, respectively. Previous studies have suggested that a homologue exists in D. immitis (DiT33), which may have potential in diagnosis of heartworm infection. In this study, the isolation and characterization of a cDNA clone encoding DiT33 is described.‡ This cDNA contains 12 bases of the nematode-specific 22 nucleotide spliced leader sequence and encodes a 26·4 kDa-protein with a high level of similarity (87–89%) to other filarial members of the family. DJT33 was over-expressed in E. coli as a fusion with the maltose-binding protein and serological analysis was performed using a panel of clinically defined dog sera. The findings of this study indicate that DiT33 is a promising antigen for the early detection of D. immitis and may be a valuable tool in the control and management of heartworm infection.

Isolation and characterization of a biologically active C2 derived oligopeptide

1982 ◽  
Vol 19 (11) ◽  
pp. 1403 ◽  
Author(s):  
M. Lopez-Trascasa ◽  
M. Moisy ◽  
E. Pirotzky ◽  
Y. Blouquit ◽  
C. Blanc ◽  
...  
Keyword(s):  
Biologically Active ◽  
Isolation And Characterization

ISOLATION AND CHARACTERIZATION OF RIBONUCLEIC ACID FROM RAT LENS

1962 ◽  
Vol 40 (1) ◽  
pp. 41-47 ◽  
Author(s):  
Anima Devi
Keyword(s):  
Amino Acids ◽  
The Other ◽  
Ocular Lens ◽  
E Coli ◽  
Isolation And Characterization ◽  
Coiled Structure ◽  
Calf Thymus ◽  
Original Procedure ◽  
Polynucleotide Chain

RNA from rat ocular lens has been isolated by a method based on Kirby's original procedure (7), but greatly modified so as to avoid any degradation of RNA by RNase during the process of its extraction from lenses. The absorption at 260 mμ of a 1.0% solution of this purified material in a 1-cm cell is 1.95. Its N/P ratio is 1.58. It has 20 to 25% activity of that of yeast-soluble RNA in accepting activated amino acids. When this RNA (like all other RNA's) is heated and cooled the polynucleotide chain can again form loops, thus suggesting a randomly coiled structure for this RNA. On the other hand, DNA preparations from calf thymus, rat liver, and E. coli showed irreversible changes when heated and cooled.

Oligo-Mucopeptide aus der Stützmembran von E. coli

1963 ◽  
Vol 18 (12) ◽  
pp. 1065-1069 ◽  
Author(s):  
W. Leutgeb ◽  
W. Weidel
Keyword(s):  
E Coli ◽  
Isolation And Characterization ◽  
Secondary Origin

Incomplete hydrolysis with lysozyme of coli mucopolymer permitted the isolation and characterization of larger mucopolymer fragments. They were shown to be chains of β(1.4) -glycosidically linked mucopeptides of known structure. The fragments contained three types of mucopeptides in all possible combinations. It was found that one of the three types is of secondary origin. The mucopolymer of actively growing cells is made up from merely two types of mucopeptidic repeating units.

scholarly journals Isolation and characterization of the cytochrome domain of flavocytochrome b2 expressed independently in Escherichia coli

1992 ◽  
Vol 283 (1) ◽  
pp. 87-90 ◽  
Author(s):  
C E Brunt ◽  
M C Cox ◽  
A G P Thurgood ◽  
G R Moore ◽  
G A Reid ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
High Field ◽  
Cytochrome B5 ◽  
Microsomal Cytochrome ◽  
E Coli ◽  
Flavocytochrome B2 ◽  
Isolation And Characterization ◽  
Exchange Rate Constant ◽  
Microsomal Cytochrome B5

The cytochrome domain of flavocytochrome b2 (L-lactate dehydrogenase) was expressed in the bacterium Escherichia coli and a purification procedure was developed. When expressed in E. coli, the b2-cytochrome domain contains protohaem IX and has an electronic absorption spectrum identical with that of the cytochrome b2 ‘core’ produced by proteolytic cleavage of the enzyme isolated from yeast. The b2-cytochrome domain isolated from E. coli has an Mr of 10,500 and a redox potential of -31 +/- 2 mV. High-field n.m.r. studies indicate pKa values for the haem propionate groups to be 4.8 and 4.6, consistent with these groups being exposed to solvent rather than buried inside the protein. Using n.m.r. spectroscopy, we have determined an electron self-exchange rate constant for the b2-cytochrome domain of 2.3 x 10(6) M-1.s-1, which is more than two orders of magnitude larger than the value obtained for microsomal cytochrome b5, a homologue of b2-cytochrome domain.

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