scholarly journals Metabolism of glycolate in Euglena gracilis. Part V. Occurrence and subcellular distribution of enzymes involved in the glycolate pathway and their physiological function in a bleached mutant of Euglena gracilis Z.

1981 ◽  
Vol 45 (1) ◽  
pp. 15-22 ◽  
Author(s):  
Akiho YOKOTA ◽  
SHOZABURO KITAOKA
1985 ◽  
Vol 49 (7) ◽  
pp. 2205-2206 ◽  
Author(s):  
Bong-Sun PARK ◽  
Aiko HIROTANI ◽  
Yoshihisa NAKANO ◽  
Shozaburo KITAOKA

1993 ◽  
Vol 35 (1) ◽  
pp. 59-61 ◽  
Author(s):  
Yuji Isegawa ◽  
Fumio Watanabe ◽  
Shozaburo Kitaoka ◽  
Yoshihisa Nakano

Microbiology ◽  
1988 ◽  
Vol 134 (1) ◽  
pp. 61-66
Author(s):  
K. HOSOTANI ◽  
T. OHKOCHI ◽  
H. INUI ◽  
A. YOKOTA ◽  
Y. NAKANO ◽  
...  

1988 ◽  
Vol 41 (6) ◽  
pp. 496-500
Author(s):  
Hirotomo OCHI ◽  
Fumio WATANABE ◽  
Shigeru SHIGEOKA ◽  
Yoshihisa NAKANO ◽  
Shozaburo KITAOKA

1988 ◽  
Vol 43 (5-6) ◽  
pp. 351-356 ◽  
Author(s):  
A. A. Juknat ◽  
D. Dörnemann ◽  
H. Senger

A low molecular weight, heat-stable factor has been purified from Euglena gracilis supernatant fraction by employing gel filtration, cation and anion exchange and paper chromatography. This endogenous compound stimulates porphobilinogenase (PBG-ase) (EC 4.3.1.8) activity, an enzyme of the porphyrin biosynthetic pathway. 10-7 ᴍ folic acid and 10-4 ᴍ 6-biopterin produced a significant activation, equivalent to 2-4 units of the purified factor. Elution patterns from the columns and fluorescence and UV absorption peaks suggest that this compound is a pteridine. This conclusion is further supported by the fact that both, folic acid and 6-biopterin can replace the action of the isolated factor on PBG-ase. The mechanism of stimulation is discussed.


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