Purification of Bacterial Thiaminase I and its Properties

2015 ◽  
pp. 116-125
Author(s):  
Kiku Murata ◽  
J. Ebata
Keyword(s):  
1968 ◽  
Vol 14 (1) ◽  
pp. 12-20 ◽  
Author(s):  
KIKU MURATA ◽  
JUNKO EBATA ◽  
MITSUKO SOMEKAWA ◽  
SUMIKO MARUKAWA
Keyword(s):  

1966 ◽  
Vol 113 (2) ◽  
pp. 331-337 ◽  
Author(s):  
H.A. Douthit ◽  
R.L. Airth
Keyword(s):  

2010 ◽  
Author(s):  
Adam D. Richardson ◽  
Shuqian Liu ◽  
Jeffrey A. Moscow

1985 ◽  
Vol 104 (3) ◽  
pp. 637-642 ◽  
Author(s):  
J. W. Boyd

SummaryKinetic studies of thiaminase I in extracts of ruminant faeces showed that the affinity for one substrate varied with the concentration of the other substrate in the manner of a two-step transfer mechanism. When the alternate substrate concentration was optimal, the apparent Michaelis constant (Km) for thiamine was 176 μΜ and the apparent Km for aniline was 3·19 mΜ. It is recommended that in routine thiaminase assays, the thiamine and aniline concentrations should be at least 1·5 and 25 mΜ, respectively. When non-saturating concentrations of thiamine are used in thiaminase assays the results should be reported as unimolecular reaction constants since the enzyme activity can be calculated only if suitable Km data have been determined.Improved radioactive and colorimetric thiaminase assays with saturating substrate concentrations gave similar results. The analytical variation of the colorimetric method was rather high but this method may be useful for laboratories which lack radioactive isotope facilities.Thiaminase assays were performed on cultures of 14 species of rumen bacteria. Only Megasphaera elsdenii had thiaminase activity and its cosubstrate specificity was different from the rumen thiaminase associated with cerebrocortical necrosis in ruminants. It was concluded that the source of rumen thiaminase in that disease has yet to be identified.


1996 ◽  
Vol 271 (7) ◽  
pp. 3445-3452 ◽  
Author(s):  
Colleen A. Costello ◽  
Neil L. Kelleher ◽  
Mitsuko Abe ◽  
Fred W. McLafferty ◽  
Tadhg P. Begley

PLoS ONE ◽  
2014 ◽  
Vol 9 (3) ◽  
pp. e92688 ◽  
Author(s):  
Clifford E. Kraft ◽  
Eric R. L. Gordon ◽  
Esther R. Angert

2012 ◽  
Vol 69 (6) ◽  
pp. 1056-1064 ◽  
Author(s):  
Catherine A. Richter ◽  
Allison N. Evans ◽  
Maureen K. Wright-Osment ◽  
James L. Zajicek ◽  
Scott A. Heppell ◽  
...  

Thiamine (vitamin B1) deficiency is a global concern affecting wildlife, livestock, and humans. In Great Lakes salmonines, thiamine deficiency causes embryo mortality and is an impediment to restoration of native lake trout ( Salvelinus namaycush ) stocks. Thiamine deficiency in fish may result from a diet of prey with high levels of thiaminase I. The discoveries that the bacterial species Paenibacillus thiaminolyticus produces thiaminase I, is found in viscera of thiaminase-containing prey fish, and causes mortality when fed to lake trout in the laboratory provided circumstantial evidence implicating P. thiaminolyticus. This study quantified the contribution of P. thiaminolyticus to the total thiaminase I activity in multiple trophic levels of Great Lakes food webs. Unexpectedly, no relationship between thiaminase activity and either the amount of P. thiaminolyticus thiaminase I protein or the abundance of P. thiaminolyticus cells was found. These results demonstrate that P. thiaminolyticus is not the primary source of thiaminase activity affecting Great Lakes salmonines and calls into question the long-standing assumption that P. thiaminolyticus is the source of thiaminase in other wild and domestic animals.


1974 ◽  
Vol 40 (7) ◽  
pp. 671-674 ◽  
Author(s):  
Tadashi ISHIHARA ◽  
Masato YASUDA
Keyword(s):  

2009 ◽  
Vol 21 (4) ◽  
pp. 229-238 ◽  
Author(s):  
Catherine A. Richter ◽  
Maureen K. Wright-Osment ◽  
James L. Zajicek ◽  
Dale C. Honeyfield ◽  
Donald E. Tillitt

Sign in / Sign up

Export Citation Format

Share Document