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

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

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 Purification and Characterization of a Cytotonic Protein Expressed In Vitro by the Live Cholera Vaccine Candidate CVD 103-HgR

2000 ◽  
Vol 68 (10) ◽  
pp. 6062-6065 ◽  
Author(s):  
Venugopal Sathyamoorthy ◽  
Robert H. Hall ◽  
Barbara A. McCardell ◽  
Mahendra H. Kothary ◽  
Susie J. Ahn ◽  
...  
Keyword(s):  
Protein S ◽  
Fluid Accumulation ◽  
Cho Cell ◽  
Purification And Characterization ◽  
Infant Mouse ◽  
Strong Homology ◽  
El Tor ◽  
Culture Supernatants

ABSTRACT Cholera vaccines developed by the deletion of CTX genes fromVibrio cholerae induce a residual reactogenicity in up to 10% of vaccinees. A novel cytotonic agent named secreted CHO cell elongating protein (S-CEP) was purified from culture supernatants of CVD 103-HgR (Levine et al., Lancet ii:467–470, 1988). Five fractionation steps yielded electrophoretically pure S-CEP with anM r of 79,000. A partially purified preparation caused fluid accumulation in the sealed infant mouse model. The amino terminus bore a unique sequence with strong homology to a cytotonic toxin of El Tor V. cholerae.

scholarly journals Purification and characterization of a novel zinc-proteinase from cultures of Aeromonas hydrophila.

1993 ◽  
Vol 268 (12) ◽  
pp. 9071-9078
Author(s):  
A.G. Loewy ◽  
U.V. Santer ◽  
M. Wieczorek ◽  
J.K. Blodgett ◽  
S.W. Jones ◽  
...  
Keyword(s):  
Aeromonas Hydrophila ◽  
Purification And Characterization

scholarly journals Purification and characterization of chitinase and chitobiase produced by Aeromonas hydrophila subsp. anaerogenes A52.

1986 ◽  
Vol 32 (1) ◽  
pp. 25-38 ◽  
Author(s):  
MINORU YABUKI ◽  
KEIJI MIZUSHINA ◽  
TOMOKO AMATATSU ◽  
AKIKAZU ANDO ◽  
TAKAAKI FUJII ◽  
...  
Keyword(s):  
Aeromonas Hydrophila ◽  
Purification And Characterization
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