Preparation and Characterization of Euglena gracilis Ribonucleic Acids with Special Reference to the Transfer RNA Fraction

Samtleben, S.; Vogt, Marguerite; Parthier, B.

doi:10.1016/s0015-3796(17)31186-1

Cited by 15 publications

(1 citation statement)

References 33 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Euglena gracilis Z cells were grown on the medium described by Cramer & Myers (1952) and modified by Padilla & James (1960), under continuous illumination at 25 °C, and harvested by centrifugation at 3500g at the end of the exponential growth phase. Euglena tRNAs were isolated as described by Meissner et al (1971).…”

Section: Methodsmentioning

confidence: 99%

Chloroplast leucyl-tRNA synthetase from Euglena gracilis. Purification, kinetic analysis, and structural characterization

Imbault¹,

Colas²,

Sarantoglou³

et al. 1981

Biochemistry

View full text Add to dashboard Cite

Euglena gracilis chloroplast leucyl-tRNA synthetase was purified to homogeneity by a series of steps including ammonium sulfate precipitation and chromatography on hydroxylapatite, DEAE-cellulose, Sepharose 6B, phosphocellulose, and Blue Dextran-Sepharose. The purified enzyme exhibits a specific activity of 1233 units/mg of protein, which is one of the highest specific activities obtained for an aminoacyl-tRNA synthetase prepared from plant cells. The enzyme has an apparent Km value of 8 x 10(-6) M for L-leucine, 1.3 x 10(-4) M for ATP, and 1.3 x 10(-6) M for tRNALeu. Chloroplast leucyl-tRNA synthetase appears to be a monomeric enzyme with a molecular weight of 100 000. The amino acid composition of chloroplast leucyl-tRNA synthetase has been determined. It is the first reported for a chloroplast aminoacyl-tRNA synthetase, and it reveals a relatively large proportion of apolar residues, as in the case of prokaryotic aminoacyl-tRNA synthetases.

show abstract

Section: Methodsmentioning

confidence: 99%

Chloroplast leucyl-tRNA synthetase from Euglena gracilis. Purification, kinetic analysis, and structural characterization

Imbault¹,

Colas²,

Sarantoglou³

et al. 1981

Biochemistry

View full text Add to dashboard Cite

show abstract

Proteolysis in Euglena gracilis

Krauspe

Scheer

Schaper

et al. 1986

Planta

View full text Add to dashboard Cite

Endoproteolytic activities (EC 3.4.22. and 23.) of cell-free extracts of Euglena gracilis, measured by autolysis and azocaseinolysis, vary considerably during the culture growth cycle. They are high in the lag phase, drop sharply up to the mid-logarithmic phase, and then rise again reaching the initial high levels in the stationary phase. This pattern has been observed for both the soluble and the particulate proteolytic activities of four cell types differing with regard to the developmental state of the chloroplast: dark-grown, light-induced, and light-grown wild-type cells, as well as light-grown apoplastic W3BUL mutant cells, all on a glucose-based medium. Therefore, the activity of the main intracellular proteinases is neither directly nor indirectly light-regulated, but seems to be controlled by the availability of nutrients. Endogenous inhibitors of proteinases could not be detected. Cysteine proteinase activity has been found in the soluble and the particulate fractions, but aspartic proteinase activity in the latter ones only. Different cysteine proteinases may be present in the two fractions, during the different growth phases, and in the four cell types studied.

show abstract

Coomassie brilliant blue G-250 dye-binding technique for determination of autolytic protein breakdown in Euglena gracilis and comparison to other methods of autolysis measurement

Krauspe

Scheer

1986

Analytical Biochemistry

View full text Add to dashboard Cite

Preparation and Characterization of Euglena gracilis Ribonucleic Acids with Special Reference to the Transfer RNA Fraction

Cited by 15 publications

References 33 publications

Chloroplast leucyl-tRNA synthetase from Euglena gracilis. Purification, kinetic analysis, and structural characterization

Chloroplast leucyl-tRNA synthetase from Euglena gracilis. Purification, kinetic analysis, and structural characterization

Proteolysis in Euglena gracilis

Coomassie brilliant blue G-250 dye-binding technique for determination of autolytic protein breakdown in Euglena gracilis and comparison to other methods of autolysis measurement

Contact Info

Product

Resources

About