Occurrence of the gene for the large subunit of ribulose-1,-5-bisphosphate carboxylase in several mutants of Euglena gracilis

1985 ◽  
Vol 37 (3) ◽  
pp. 245-249 ◽  
Author(s):  
Georges Freyssinet ◽  
Martine Freyssinet ◽  
Michel Lebrun
Keyword(s):  
Euglena Gracilis ◽  
Large Subunit ◽  
Bisphosphate Carboxylase ◽  
Ribulose 1

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.

Changes in the heterogeneity of ribulosebisphosphate carboxylase–oxygenase in winter rye induced by cold hardening

1982 ◽  
Vol 60 (9) ◽  
pp. 897-903 ◽  
Author(s):  
N. P. A. Huner ◽  
D. B. Hayden
Keyword(s):  
Large Subunit ◽  
Cold Hardening ◽  
Winter Rye ◽  
Charge Heterogeneity ◽  
Two Dimensional Gel Electrophoresis ◽  
Bisphosphate Carboxylase ◽  
Ribulose 1 ◽  
Ribulosebisphosphate Carboxylase ◽  
Quaternary Structures ◽  
Molecular Weight Heterogeneity

The quaternary structures of ribulose-1, 5-bisphosphate carboxylase–oxygenase from cold-hardened and unhardened Puma rye were examined by two-dimensional gel electrophoresis according to the method of O'Farrell. The results indicate that major changes in charge heterogeneity occur in the large subunit of this enzyme during growth at cold-hardening temperatures. The extent of charge heterogeneity decreased upon adaptation of Puma rye to cold-hardening temperatures. In addition to charge heterogeneity, molecular weight heterogeneity was also evident in the large subunit polypeptides of the enzyme from cold-hardened and unhardened Puma rye.

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