Chromatographic separation, of extracellular acid phosphatase of tobacco cells cultured under Pi-supplied and omitted conditions

1977 ◽  
Vol 18 (2) ◽  
pp. 413-420 ◽  
Author(s):  
Yaéko Ninomiya ◽  
Katsuji Ueki ◽  
Sitiro Sato
2008 ◽  
Vol 69 (14) ◽  
pp. 2546-2551 ◽  
Author(s):  
Rumi Kaida ◽  
Takahisa Hayashi ◽  
Takako S. Kaneko

1979 ◽  
Vol 20 (8) ◽  
pp. 1489-1499 ◽  
Author(s):  
Hiromitsu Nakajima ◽  
Takao Yokota ◽  
Takashi Matsumoto ◽  
Masao Noguchi ◽  
Nobutaka Takahashi

1996 ◽  
Vol 16 (2-3) ◽  
pp. 207-213 ◽  
Author(s):  
J. Fiedurek ◽  
B. Pluta ◽  
J. Szczodrak ◽  
J. Jamroz

2009 ◽  
Vol 150 (4) ◽  
pp. 1822-1830 ◽  
Author(s):  
Rumi Kaida ◽  
Yumi Satoh ◽  
Vincent Bulone ◽  
Yohko Yamada ◽  
Tomomi Kaku ◽  
...  

1996 ◽  
Vol 16 (1) ◽  
pp. 65-71 ◽  
Author(s):  
B. Tchorbanov ◽  
P. Aleksieva ◽  
N. Dambadarja ◽  
G. Dyulgerova

1982 ◽  
Vol 2 (1) ◽  
pp. 76-81
Author(s):  
M Gottlieb ◽  
D M Dwyer

An extracellular acid phosphatase was detected in the growth media of Leishmania donovani promastigotes. The enzyme was released at all stages of the growth cycle and in amounts which accounted for 90% of the total amount of this enzyme in the culture. The exoenzyme exhibited a pH optimum of 4.5 to 5.0 and was active with a variety of organic phosphates. The enzymatic activity was excluded from Sephacryl S-300 and was retained by ultrafilters with nominal molecular weight cutoffs of up to 300,000. The results of comparative studies indicated that the extracellular enzyme was distinct from a surface membrane-bound acid phosphatase of L. donovani promastigotes which has been previously described.


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