l casei atcc 27139 (ATCC)
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L Casei Atcc 27139, supplied by ATCC, used in various techniques. Bioz Stars score: 96/100, based on 125 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 96 stars, based on 125 article reviews
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1) Product Images from "Transposon Mutagenesis of Probiotic Lactobacillus casei Identifies asnH , an Asparagine Synthetase Gene Involved in Its Immune-Activating Capacity"
Article Title: Transposon Mutagenesis of Probiotic Lactobacillus casei Identifies asnH , an Asparagine Synthetase Gene Involved in Its Immune-Activating Capacity
Journal: PLoS ONE
doi: 10.1371/journal.pone.0083876
Figure Legend Snippet: Summary of relative sensitivities to J1 phage infection and predicted transposon insertion loci of J1 phage-resistant mutant.
Techniques Used: Infection, Mutagenesis
Figure Legend Snippet: Heat-killed preparations of L. casei ATCC 27139 or isogenic Tn 5 insertion mutants (800 µg) were injected i.v. into BALB/c mice 6 days before an i.v. challenge with L. monocytogenes (2.0×10 6 CFU/mouse). Six mice per group were dissected 24 h after the challenge, and viable Listeria were detected in spleens. Columns: white, saline; black, L. casei wild-type; slashed, L. casei J1 phage-resistant mutant; gray, L. casei asnH mutant complemented with the cloned asnH . Results are depicted as the means ± standard deviations (SD). Statistical significance was calculated using the Student's t -test. Significant differences indicated between the control and treated groups. ***, p <0.001.
Techniques Used: Injection, Mutagenesis, Clone Assay
Figure Legend Snippet: Heat-killed preparations of L. casei ATCC 27139 or isogenic Tn 5 insertion mutants (800 µg) were injected i.v. into BALB/c mice. Six mice per group were sacrificed 8 h after injection, and IL-12 (A), TNF-α (B), and IFN-γ (C) proteins were measured from spleen homogenates by ELISA. Columns: white, saline; black, L. casei wild-type; slashed, L. casei J1 phage-resistant mutant; gray, L. casei asnH mutant complemented with the cloned asnH . Results are depicted as the means ± standard deviations (SD). Statistical significance was calculated using the Student's t -test. Significant differences indicated between the control and treated groups. ***, p <0.001.
Techniques Used: Injection, Enzyme-linked Immunosorbent Assay, Mutagenesis, Clone Assay
Figure Legend Snippet: (A) Protein sequence alignment was performed using the GENETYX program. Solid boxes indicate highly conserved regions. Regions containing residues important for enzymatic activities are shown in detail (identical residues are indicated by boldface type). The first methionine was consistently included in the numbering and was designated Met-1. Asterisks indicate mutated residues in this study that were critical to glutaminase or synthetase activities. (B) Recombinant AsnH WT , mutant AsnH C2S , and mutant AsnH D265N (0.1 µg) were examined using the glutaminase activity test. Five microliters of a reaction mixture (initial volume, 50 µl) were quenched at 30 min to estimate glutamic acid concentration. Glutaminase activity was monitored in the presence of aspartic acid or cell wall extracts of ATCC 27139, ATP or AMP–PNP plus cell wall extracts. Results are depicted as the means ± standard deviations (SD). Statistical significance was calculated using the Student's t -test. Significant differences indicated between the control and treated groups. ***, p <0.001.
Techniques Used: Sequencing, Recombinant, Mutagenesis, Activity Assay, Concentration Assay
Figure Legend Snippet: Amino acid compositions in peptidoglycans and lysozyme MICs of J1 phage-resistant mutants.
Techniques Used:
Figure Legend Snippet: Relative sensitivities to J1 phage infection among MNNG-induced J1 phage-resistant mutants.
Techniques Used: Infection
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