Characterization of an antimicrobial peptide produced by Bacillus subtilis subsp. spizezinii showing inhibitory activity towards Haemophilus parasuis

Microbiology ◽  
2013 ◽  
Vol 159 (Pt_5) ◽  
pp. 980-988 ◽  
Author(s):  
Mário Lettieri Teixeira ◽  
Andréia Dalla Rosa ◽  
Adriano Brandelli
Keyword(s):  
Bacillus Subtilis ◽  
Antimicrobial Peptide ◽  
Inhibitory Activity ◽  
Haemophilus Parasuis ◽  
Subtilis Subsp

Recombinant expression and characterization of XynD from Bacillus subtilis subsp. subtilis ATCC 6051: a GH 43 arabinoxylan arabinofuranohydrolase

2007 ◽  
Vol 75 (6) ◽  
pp. 1309-1317 ◽  
Author(s):  
Tine M. Bourgois ◽  
Valerie Van Craeyveld ◽  
Steven Van Campenhout ◽  
Christophe M. Courtin ◽  
Jan A. Delcour ◽  
...  
Keyword(s):  
Bacillus Subtilis ◽  
Recombinant Expression ◽  
Subtilis Atcc ◽  
Arabinoxylan Arabinofuranohydrolase ◽  
Subtilis Subsp

scholarly journals Organization and characterization of genetic regions in Bacillus subtilis subsp. krictiensis ATCC55079 associated with the biosynthesis of iturin and surfactin compounds

PLoS ONE ◽  
2017 ◽  
Vol 12 (12) ◽  
pp. e0188179 ◽  
Author(s):  
Young Tae Kim ◽  
Byung Keun Park ◽  
Sung Eun Kim ◽  
Won Jung Lee ◽  
Jae Sun Moon ◽  
...  
Keyword(s):  
Bacillus Subtilis ◽  
Subtilis Subsp

Characterization of an Abnormal Antithrombin (Milano 2) with Defective Thrombin Binding

1986 ◽  
Vol 56 (03) ◽  
pp. 349-352 ◽  
Author(s):  
A Tripodi ◽  
A Krachmalnicoff ◽  
P M Mannucci
Keyword(s):  
Venous Thromboembolism ◽  
Active Site ◽  
Inhibitory Activity ◽  
Antithrombin Iii ◽  
Factor Xa ◽  
Molecular Defect ◽  
Affinity Adsorption ◽  
Italian Family ◽  
Crossed Immunoelectrophoresis

SummaryFour members of an Italian family (two with histories of venous thromboembolism) had a qualitative defect of antithrombin III reflected by normal antigen concentrations and halfnormal antithrombin activity with or without heparin. Anti-factor Xa activities were consistently borderline low (about 70% of normal). For the propositus’ plasma and serum the patterns of antithrombin III in crossed-immunoelectrophoresis with or without heparin were indistinguishable from those of normal plasma or serum. A normal affinity of antithrombin III for heparin was documented by heparin-sepharose chromatography. Affinity adsorption of the propositus’ plasma to human α-thrombin immobilized on sepharose beads revealed defective binding of the anti thrombin III to thrombin-sepharose. Hence the molecular defect of this variant appears to be at the active site responsible for binding and neutralizing thrombin, thus accounting for the low thrombin inhibitory activity.

The Study of Bacillus Subtils Antimicrobial Activity on Some of the Pathological Isolates

2019 ◽  
Vol 9 (02) ◽  
Author(s):  
Hussein A Kadhum ◽  
Thualfakar H Hasan2
Keyword(s):  
Staphylococcus Aureus ◽  
Pseudomonas Aeruginosa ◽  
Antimicrobial Activity ◽  
Bacillus Subtilis ◽  
Bacterial Growth ◽  
Broad Spectrum ◽  
Inhibitory Activity ◽  
Bacterial Pathogens ◽  
Inhibitory Ability ◽  
Selection Of

The study involved the selection of two isolates from Bacillus subtilis to investigate their inhibitory activity against some bacterial pathogens. B sub-bacteria were found to have a broad spectrum against test bacteria such as Staphylococcus aureus and Pseudomonas aeruginosa. They were about 23-30 mm and less against Klebsiella sp. The sensitivity of some antibodies was tested on the test samples. The results showed that the inhibitory ability of bacterial growth in the test samples using B. subtilis extract was more effective than the antibiotics used.

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