Limitations of using extracellular alkaline phosphatase activities as a general indicator for describing P deficiency of phytoplankton in Chinese shallow lakes

2009 ◽  
Vol 22 (1) ◽  
pp. 33-41 ◽  
Author(s):  
Xiuyun Cao ◽  
Chunlei Song ◽  
Yiyong Zhou
1980 ◽  
Vol 26 (7) ◽  
pp. 833-838 ◽  
Author(s):  
Hiromi Kobori ◽  
Nobuo Taga

Extracellular alkaline phosphatase produced by a marine Pseudomonas was purified to electrophoretic homogeneity. The molecular weight of the enzyme was estimated to be 100 000. The enzyme had maximal activity at pH 11.5. The enzyme was completely inhibited by 1 mM EDTA. However, divalent cations reversed the enzyme inhibition and their order of effectiveness on the reaction was Zn2+ > Ca2+ > Mn2+ > Mg2+ > Sr2+ > Co2+. The enzyme activity was affected by the species of anion whose order of effectiveness was demonstrated to follow the lyotrophic series, Cl− > Br− > NO3−> ClO4− > SCN−. The activity of phosphatase was accelerated linearly by increased pressure until up to 1000 atm (1 atm = 101.325 kPa), and the enzyme activity at 1000 atm was 3.2 times higher than that at 1 atm.


Author(s):  
Michio Ogawa ◽  
Kenjiro Iwaki ◽  
Naoko Saito ◽  
Shigenori Tanaka ◽  
Goro Kosaki

Serum succinyltrialanine p-nitroanilide hydrolysing activity was elevated in patients with hepatobiliary diseases. The highest activities were seen in acute cholangitis and intrahepatic cholestasis. The change in succinyltrialanine p-nitroanilide hydrolysing activity was closely associated with those in γ-glutamyltranspeptidase and alkaline phosphatase activities. In some cases, however, the former was more sensitive than the latter.


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