scholarly journals Study of Ribulose 1, 5-Bisphosphate Carboxylase from Sulfobacillus acidophilus Strain NY-1 Isolated from Lignite Mines

2020 ◽  
Vol 18 (4) ◽  
pp. 356-362
Author(s):  
Jenny Angel Stanislaus ◽  
◽  
Dhandapani Ramamoorthy ◽  
Keyword(s):  
Bisphosphate Carboxylase ◽  
Ribulose 1 ◽  
Lignite Mines

Three-dimensional distribution of ribulose-1, 5-bisphosphate carboxylase/oxygemase during the early development of proplastids in dark-grown Euglena cells transferred to an inorganic medium

1990 ◽  
Vol 48 (3) ◽  
pp. 906-907
Author(s):  
Tomoko Ehara ◽  
Shuji Sumida ◽  
Tetsuaki Osafune ◽  
Eiji Hase
Keyword(s):  
Cell Suspension ◽  
Euglena Gracilis ◽  
Carbon Materials ◽  
Three Dimensional ◽  
Peripheral Region ◽  
Plastid Development ◽  
Bisphosphate Carboxylase ◽  
Inorganic Medium ◽  
Ribulose 1 ◽  
Dimensional Distribution

As shown previously, Euglena cells grown in Hutner’s medium in the dark without agitation accumulate wax as well as paramylum, and contain proplastids showing no internal structure except for a single prothylakoid existing close to the envelope. When the cells are transferred to an inorganic medium containing ammonium salt and the cell suspension is aerated in the dark, the wax was oxidatively metabolized, providing carbon materials and energy 23 for some dark processes of plastid development. Under these conditions, pyrenoid-like structures (called “pro-pyrenoids”) are formed at the sites adjacent to the prolamel larbodies (PLB) localized in the peripheral region of the proplastid. The single prothylakoid becomes paired with a newly formed prothylakoid, and a part of the paired prothylakoids is extended, with foldings, in to the “propyrenoid”. In this study, we observed a concentration of RuBisCO in the “propyrenoid” of Euglena gracilis strain Z using immunoelectron microscopy.

Roles of the Large and Small Subunits of Ribulose-1, 5-Bisphosphate Carboxylase in the Activation by CO2 and Mg2+1

1979 ◽  
Vol 85 (4) ◽  
pp. 923-930 ◽  
Author(s):  
Hirokazu KOBAYASHI ◽  
Tetsuko TAKABE ◽  
Mikio NISHIMURA ◽  
Takashi AKAZAWA
Keyword(s):  
Bisphosphate Carboxylase ◽  
Ribulose 1

Ribulose-1,5-bisphosphate Carboxylase-Oxygenase: New Aspects Respective the pH-Dependance of the Carboxylation Reaction

1983 ◽  
Vol 38 (3-4) ◽  
pp. 243-246 ◽  
Author(s):  
P. Braun ◽  
J. Bode ◽  
A. Wild
Keyword(s):  
Crude Enzyme ◽  
Activity Profile ◽  
Reaction Conditions ◽  
Carboxylase Activity ◽  
Bisphosphate Carboxylase ◽  
Ribulose 1 ◽  
Substrate Concentrations

The investigation was directed towards the effects of reaction conditions, substrates and pH on the carboxylation reaction of ribulose-1 ,5-bisphosphate carboxylase-oxygenase in the crude enzyme extracts from several plants. Optimal substrate concentrations (HCO3- and RubP) were determined. The highest carboxylase activity was attained with Tris/HCl buffer. The pH activity profile was quite sharp with an optimum at pH 7.8. Purified and crystallized carboxylase yielded a broad optimum curve under the same reaction conditions

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