Characteristics of the Chloroplast Import of a Precursor to the Nuclear-Encoded Extrinsic 30-KDA Protein of PS II in Euglena Gracilis Z

1992 ◽  
pp. 177-180
Author(s):  
Junko Inagaki ◽  
Ikuo Kuroda ◽  
Yasusi Yamamoto
1982 ◽  
Vol 37 (3-4) ◽  
pp. 256-259 ◽  
Author(s):  
F. Schuler ◽  
P. Brandt ◽  
W. Wießner

Abstract An improved method for isolation of (photosystem II)-particles from Euglena gracilis, strain Z was established. PS II-particles isolated by ultrasonic treatment and following differential centrifugation show fluorescence emission and absorption spectra identical with in vivo properties of Euglena gracilis. These PS II-particles have only PS II-activity and contain CP a, the typical chlorophyll-protein-complex of PS II. No contamination of PS I-components are detectable.


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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