Nomenclature Abstract for Beneckea natriegens (Payne et al. 1961) Baumann et al. 1971 (Approved Lists 1980).

2003 ◽  
Author(s):  
Charles Thomas Parker ◽  
Dorothea Taylor ◽  
George M Garrity
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1977 ◽  
Vol 100 (1) ◽  
pp. 5-13 ◽  
Author(s):  
D. F. NIVEN ◽  
P. A. COLLINS ◽  
C. J. KNOWLES




1977 ◽  
Vol 115 (2) ◽  
pp. 135-142 ◽  
Author(s):  
John D. Linton ◽  
David E. F. Harrison ◽  
Alan T. Bull


1981 ◽  
Vol 129 (2) ◽  
pp. 119-122 ◽  
Author(s):  
J. D. Linton ◽  
K. Griffiths ◽  
M. Gregory


1988 ◽  
Vol 16 (5) ◽  
pp. 767-767 ◽  
Author(s):  
A. C. FAIRCLOUGH ◽  
B. DAVIS ◽  
D. JOHNSON ◽  
P. LOXLEY ◽  
J. MILLS ◽  
...  




1981 ◽  
Vol 27 (10) ◽  
pp. 1053-1059 ◽  
Author(s):  
Karamchand Ramotar ◽  
Michael A. Pickard

Adenylate kinase (EC 2.7.4.3) has been purified 484-fold from extracts of Vibrio natriegens to a specific activity of 1350 μmol ADP formed∙min−1∙mg protein−1. The preparation was 97% pure as judged by gel electrophoresis and exhibited molecular weight values of 29 000 by gel filtration and 32 000 by SDS–gel electrophoresis. The isoelectric point was at pH 4.7. Only ATP (Km 0.067 mM), ADP (Km 0.45 mM), and AMP (Km 0.12 mM) exhibited high activity as substrates, though dATP or dAMP could serve as cosubstrates with AMP or ATP, respectively, at reduced rates. The equilibrium constant in the direction of ATP formation was 1.09, and the pH optimum in both directions was broad, from pH 7.2 to pH 7.6. Enzyme activity was sensitive to the thiolalkylating agents iodacetamide and p-chloromercuriphenyl sulfonate.



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