Expression, Purification, and Characterization of Hemolytic Toxin from Virulent Aeromonas hydrophila

2016 ◽  
Vol 48 (3) ◽  
pp. 531-536 ◽  
Author(s):  
Jing Dong ◽  
Jing Ruan ◽  
Ning Xu ◽  
Yibin Yang ◽  
Xiaohui Ai
Keyword(s):  
Aeromonas Hydrophila ◽  
Purification And Characterization ◽  
Hemolytic Toxin ◽  
Virulent Aeromonas Hydrophila

Purification and characterization of an Aeromonas hydrophila hemolysin.

1986 ◽  
Vol 24 (2) ◽  
pp. 228-232 ◽  
Author(s):  
T Asao ◽  
S Kozaki ◽  
K Kato ◽  
Y Kinoshita ◽  
K Otsu ◽  
...  
Keyword(s):  
Aeromonas Hydrophila ◽  
Purification And Characterization

scholarly journals Identification and characterization of virulent Aeromonas hydrophila Ah17 from infected Channa striata in river Cauvery and in vitro evaluation of shrimp chitosan

2020 ◽  
Vol 8 (2) ◽  
pp. 1272-1283 ◽  
Author(s):  
Vignesh Samayanpaulraj ◽  
Muthukumar Sivaramapillai ◽  
Sankara Naynar Palani ◽  
Krishnaveni Govindaraj ◽  
Vijay Velu ◽  
...  
Keyword(s):  
Aeromonas Hydrophila ◽  
In Vitro Evaluation ◽  
Channa Striata ◽  
Virulent Aeromonas Hydrophila ◽  
Identification And Characterization

scholarly journals B24 Purification and characterization of hemolytic toxin from Actineria villosa

2002 ◽  
Vol 53 (Supplement) ◽  
pp. 60
Author(s):  
G. Uechi ◽  
H. Toma ◽  
Y. Sato ◽  
T. Arakawa
Keyword(s):  
Purification And Characterization ◽  
Hemolytic Toxin

Partial purification and characterization of an extracellular proteinase from Aeromonas hydrophila strain A4

1988 ◽  
Vol 55 (1) ◽  
pp. 97-107 ◽  
Author(s):  
Efstathios Alichanidis
Keyword(s):  
Aeromonas Hydrophila ◽  
Deae Cellulose ◽  
Enzymic Activity ◽  
Partial Purification ◽  
Significant Activity ◽  
Metal Chelators ◽  
Purification And Characterization ◽  
Tris Maleate ◽  
Ph Range

SummaryAn extracellular metalloproteinase from Aeromonas hydrophila strain A4, isolated from milk, was purified by a factor of 300 by chromatogrpahy on DEAE-cellulose and Sephadex G-150. The enzyme had a mol. wt of 43000 and contained 2 g atom Ca/mol. It was active over a pH range 4·8–9·5 and had optimum activity on casein at pH 7·0 with Km = 0·17 mM. It was strongly inactivated by metal chelators and the apoenzyme was fully reactivated with Ca2+, Mn2+ or Co2+. Heavy metal ions such as Ag+, Hg2+, Fe2+, Zn2+, Cd2+, Ni2+ and Cu2+ totally or partly inactivated the enzymic activity at 5 mM concentration. The enzyme was not inactivated by diisopropylfluorophosphate, soyabean trypsin inhibitor or sulphydryl group reagents. It was optimally active at 45 °C; above 50 °C activity declined rapidly, but significant activity persisted at 4 °C. It was heat labile in phosphate or Tris-maleate buffer but exogenous Ca2+ afforded protection.

scholarly journals Isolation and characterization of bacteriophages against virulent Aeromonas hydrophila

2020 ◽  
Vol 20 (1) ◽  
Author(s):  
Jin Liu ◽  
Shanshan Gao ◽  
Yuhao Dong ◽  
Chengping Lu ◽  
Yongjie Liu
Keyword(s):  
Aeromonas Hydrophila ◽  
Isolation And Characterization ◽  
Virulent Aeromonas Hydrophila

Purification and characterization of a CHO cell-elongating toxin produced by Aeromonas hydrophila

1995 ◽  
Vol 19 (1) ◽  
pp. 1-9 ◽  
Author(s):  
Barbara A. McCardell ◽  
Joseph M. Madden ◽  
Mahendra H. Kothary ◽  
Venugopal Sathyamoorthy
Keyword(s):  
Aeromonas Hydrophila ◽  
Cho Cell ◽  
Purification And Characterization
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