Protein Synthesis During Oxygen Deprivation in Cotton

1996 ◽  
Vol 23 (3) ◽  
pp. 341 ◽  
Author(s):  
AA Millar ◽  
ES Dennis
Keyword(s):  
Molecular Weight ◽  
Protein Synthesis ◽  
Gel Electrophoresis ◽  
Major Part ◽  
Oxygen Deprivation ◽  
Two Dimensional ◽  
Root Tips ◽  
Two Dimensional Gel Electrophoresis ◽  
Molecular Masses ◽  
Adh Activity

The alteration of protein synthesis induced by oxygen deprivation has been examined in the root tips of cotton (Gossypium hirsutum cv. Siokra), a plant that is intolerant to anoxia. Using [35S]methionine labelling and two-dimensional gel electrophoresis it was demonstrated that 14 major polypeptides are being selectively synthesised during oxygen deprivation. These polypeptides have been designated the cotton anaerobic polypeptides (ANPs), and have estimated molecular masses that correspond to molecular masses of ANPs from other plant species. However, compared to maize, several of the major molecular weight classes are absent, suggesting that the response to oxygen deprivation in cotton is simpler than that of maize. Alcohol dehydrogenase (ADH) activity is induced by oxygen deprivation. Using western analysis we have determined that this increase in activity is correlated with the accumulation of the ADH polypeptide and that three of the major cotton ANPs are ADH, including the most intensely labelled ANP, demonstrating that the synthesis of ADH constitutes a major part of the response in cotton.

Identification and quantitation of elongation factor EF-P in Escherichia coli cell-free extracts

1980 ◽  
Vol 58 (11) ◽  
pp. 1312-1314 ◽  
Author(s):  
Gynheung An ◽  
Bernard R. Glick ◽  
James D. Friesen ◽  
M. Clelia Ganoza
Keyword(s):  
Escherichia Coli ◽  
Molecular Weight ◽  
Protein Synthesis ◽  
Gel Electrophoresis ◽  
Ribosomal Proteins ◽  
Elongation Factor ◽  
Peptide Bond ◽  
Two Dimensional ◽  
Two Dimensional Gel Electrophoresis

EF-P, an elongation factor that stimulates peptide bond synthesis in vitro with some aminoacyl-tRNAs, has been identified by two-dimensional gel electrophoresis and the cellular content at three points in the growth curve has been measured. The molecular weight of EF-P is estimated to be 21 000. EF-P is a slightly acidic protein whose isoelectric point is close to RNA polymerase subunit α. The amount of EF-P present in Escherichia coli is about [Formula: see text]that of EF-G and the level is independent of the stage of cell growth; there is about one EF-P per 10 ribosomes. It is also shown that a highly purified preparation of EF-P is free of all known protein synthesis factors and ribosomal proteins.

Two-dimensional gel electrophoresis of human brain proteins. I. Technique and nomenclature of proteins.

1982 ◽  
Vol 28 (4) ◽  
pp. 782-789 ◽  
Author(s):  
D E Comings
Keyword(s):  
Human Brain ◽  
Gel Electrophoresis ◽  
Urea Solution ◽  
Two Dimensional ◽  
Two Dimensional Gel Electrophoresis ◽  
Polypeptide Patterns ◽  
Normal Individuals ◽  
Molecular Masses ◽  
Group B ◽  
The Individual

Abstract To understand at a molecular level the basis of the normal and pathological genetic differences between individuals it is necessary to begin a detailed two-dimensional gel electrophoretic mapping of the proteins of the human brain in normal individuals and those with various genetic neurological disorders. The present study is an examination of the polypeptide patterns of extracts of the human brain made with 9 mol/L urea solution. Details of the technique and the nomenclature of the patterns obtained are presented. the gels are separated into 20 sub-sections, based on standards with known molecular masses and isoelectric points. Groups of polypeptides within these sub-sections are identified by a number and a letter; the individual proteins are identified by a number. Thus, protein 1 in subsection 8, group b, would be designated 8b: 1. Subsequent papers in this series identify many of these proteins; show which proteins belong to the cytosol, synaptosome, myelin, and other brain fractions; show how these patterns vary between normal individuals and those with different neurological and psychiatric conditions; examine the effect of severe gliosis; and present the results of non-equilibrium gel electrophoresis for the more basic proteins.

scholarly journals Multiple forms of tubulin in the cytoskeletal and flagellar microtubules of polytomella

1981 ◽  
Vol 91 (2) ◽  
pp. 352-360 ◽  
Author(s):  
TW McKeithan ◽  
JL Rosenbaum
Keyword(s):  
Protein Synthesis ◽  
Gel Electrophoresis ◽  
Cold Temperature ◽  
Two Dimensional ◽  
Multiple Forms ◽  
Cytoplasmic Fraction ◽  
Two Dimensional Gel Electrophoresis ◽  
Brain Tubulin ◽  
Β Tubulin

The alga polytomella contains several organelles composed of microtubules, including four flagella and hundreds of cytoskeletal microtubules. Brown and co-workers have shown (1976. J. Cell Biol. 69:6-125; 1978, Exp. Cell Res. 117: 313-324) that the flagella could be removed and the cytoskeletans dissociated, and that both structures could partially regenerate in the absence of protein synthesis. Because of this, and because both the flagella and the cytoskeletons can be isolated intact, this organism is particularly suitable for studying tubulin heterogeneity and the incorporation of specific tubulins into different microtubule-containing organelles in the same cell. In order to define the different species of tubulin in polytonella cytoplasm, a (35)S- labeled cytoplasmic fraction was subjected to two cycles of assembly and disassembly in the presence of unlabeled brain tubulin. Comparison of the labeled polytomella cytoplasmic tubulin obtained by this procedure with the tubulin of isolated polytomella flagella by two-dimensional gel electrophoresis showed that, whereas the β-tubulin from both cytoplasmic and flagellar tubulin samples comigrated, the two α-tubulins had distinctly different isoelectic points. As a second method of isolating tubulin from the cytoplasm, cells were gently lysed with detergent and intact cytoskeletons obtained. When these cytoskeletons were exposed to cold temperature, the proteins that were released were found to be highly enriched in tubulin; this tubulin, by itself, could be assembled into microtubules in vitro. The predominant α-tubulin of this in vitro- assembled cytoskeletal tubulin corresponded to the major cytoplasmic α-tubulin obtained by coassembly of labeled polytomella cytoplasmic extract with brain tubulin and was quite distinct from the α-tubulin of purified flagella. These results clearly show that two different microtubule-containing organelles from the same cell are composed of distinct tubulins.

scholarly journals Variations in the Methionine-rich Protein Composition of the Genus Arachis1

1984 ◽  
Vol 11 (1) ◽  
pp. 1-3 ◽  
Author(s):  
Sheikh M. Basha ◽  
Sunil K. Pancholy
Keyword(s):  
Molecular Weight ◽  
Gel Electrophoresis ◽  
Protein Composition ◽  
Electrophoretic Analysis ◽  
Two Dimensional ◽  
Weight Group ◽  
Two Dimensional Gel Electrophoresis ◽  
One Dimensional ◽  
Molecular Weights ◽  
Isoelectric Points

Abstract Methionine-rich proteins (MRP) from seeds of different species of the Genus Arachis were isolated and analyzed by gel electrophoresis to detect possible compositional differences. One-dimensional gel electrophoretic analysis showed presence of quantitative and qualitative variations among the MRP-fractions. Following two-dimensional gel electrophoresis, the MRP-fractions were found to contain three groups of polypeptides with apparent molecular weights of approximately 21,000; 19,000 and 16,000, and isoelectric points between 5.1 and 5.8. Within each molecular weight group the number of polypeptides varied between 1 and 3.

Fibrin-I Degradation Products with a Molecular Weight Higher than That of Fibrinogen

1973 ◽  
Vol 29 (01) ◽  
pp. 122-129 ◽  
Author(s):  
René von Hugo ◽  
Henner Graeff
Keyword(s):  
Molecular Weight ◽  
Gel Electrophoresis ◽  
Degradation Products ◽  
Gel Filtration ◽  
Agarose Gel ◽  
Two Dimensional ◽  
Plasma Clot ◽  
Two Dimensional Gel Electrophoresis ◽  
Parent Molecule

SummaryThe observation of intravascular lysis of fibrin deposits and of fibrinogen derivatives with a molecular weight higher than the parent molecule in human cases of disseminated intravascular coagulation (DIC) initiated the following in vitro study. Following streptokinase induced plasma clot solubilization fibrinogen derivatives were investigated after ß-alanine precipitation of the plasma samples by polyacrylamide (PAA) gel electrophoresis, intra gel immunoprecipitation, two dimensional gel electrophoresis and by agarose gel filtration. Three fibrin-i degradation products were observed and characterized according to their relative electrophoretic mobility in 5% PAA gel: 0.23, 0.35, 0.46 (fibrinogen: 0.43) x 10-5 cm2/V x sec. They could also be demonstrated after electrophoresis in the presence of 5 M urea. Agarose gel filtration yielded one peak at 180 ml of effluent volume. The 0.23 derivative was eluted in the peak fractions, whilst the 0.35 and 0.46 derivatives were eluted together at approximately 201 ml of the effluent volume (fibrinogen: 225 ml). This indicates, that the three fibrin-i degradation products described are molecular entities with molecular weights higher than fibrinogen and, that the 0.46 derivative has an increased charge/molecular size ratio in comparison with fibrinogen. Corresponding data were obtained by two dimensional gel electrophoresis in gels of different pore size.

Changes in patterns of protein synthesis in axolotl oocytes during progesterone-induced maturation

Development ◽  
1986 ◽  
Vol 92 (1) ◽  
pp. 103-113
Author(s):  
Jean Gautier ◽  
Renée Tencer
Keyword(s):  
Protein Synthesis ◽  
Protein Phosphorylation ◽  
Cholera Toxin ◽  
Oocyte Maturation ◽  
Gel Electrophoresis ◽  
De Novo ◽  
Protein Pattern ◽  
Ambystoma Mexicanum ◽  
Two Dimensional ◽  
Two Dimensional Gel Electrophoresis

Patterns of protein phosphorylation and synthesis during axolotl (Ambystoma mexicanum) oocyte maturation were studied by incorporation of [32P]orthophosphate and [35S]methionine into polypeptides, followed by two-dimensional gel electrophoresis. Various alterations were observed after progesterone treatment: de novo appearance of [35S]methionine-labelled polypeptides, a quantitative increase in previously synthesized proteins and a quantitative decrease in or disappearance of other previously synthesized proteins. Changes in 32P- and 35S-labelling were observed very early during maturation. Neither prior oocyte enucleation nor α-amanitin treatment had a significant effect on these changes. Stimulation with MPF provided the same final protein pattern as PG treatment. However, cholera toxin inhibited all the changes seen during maturation. Comparisons between the patterns of [35S]methionine- and [32P]phosphatelabelling provide further information on the biochemical events that take place during oocyte maturation.

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