Two dimensional acrylamide gel electrophoresis of wheat leaf cytoplasmic and chloroplast ribosomal proteins

Jones, B. L.; Nagabhushan, N.; Gulyás, Anna; Zalik, Saul

doi:10.1016/0014-5793(72)80332-6

Cited by 22 publications

(4 citation statements)

References 11 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…As may be seen from Table I and Figure 1, Manitou had the largest number of ribosomal proteins and barley the least. Because of the change in duration of the electrophoretic runs, the protein pattern was somewhat different, but the number of basic and acidic proteins found in the cytoplasmic ribosomal proteins of Manitou wheat were the same as reported by us previously (5 (5), all of the species examined contained acidic ribosomal proteins but the intensities of the spots varied considerably (Fig. 1).…”

Section: Methodssupporting

confidence: 75%

“…For separation of the ribosomal proteins, the modified method of Kaltschmidt and Wittmann (8) was used. However, the protein samples were applied to two separate gels in the first dimension and were electrophoresed towards the cathode and the anode separately (5). Methyl green and bromophenol blue were coelectrophoresed with the basic and acidic proteins, respectively, to enable runs with uniform migration distances in the first dimension.…”

Section: Methodsmentioning

confidence: 99%

“…Previous studies in our laboratory (5) employing two-dimensional electrophoresis to compare proteins of 70S and 80S wheat leaf ribosomes revealed that the proteins of chloroplast and cytoplasmic ribosomes differed in numbers, in their relative amounts, and in electrophoretic mobilities. The cytoplasmic ribosomes contained more proteins than have been reported for animals, and the chloroplast ribosomes contained more than have been reported for prokaryotes.…”

mentioning

confidence: 93%

See 2 more Smart Citations

Comparison of Plant Cytoplasmic Ribosomal Proteins by Two-Dimensional Polyacrylamide Gel Electrophoresis

Nagabhushan

Gulyás²,

Zalik³

1974

Plant Physiol.

Self Cite

View full text Add to dashboard Cite

The electrophoretic mobilities of the cytoplasmic ribosomal proteins of several species of plants were compared using twodimensional electrophoresis. The total number of proteins as well as the number of acidic and basic proteins in individual species varied markedly. Of the species examined, Triticum aestivum had the highest number of basic cytoplasmic ribosomal proteins and Hordeum vulgare had less than half as many. However, marked similarities were noted in the electrophoretic mobilities of many of the proteins, especially for wheat, rye, and barley and for peas and beans. There was a statistically significant positive correlation between the numbers of basic proteins in the species and their chromosome number.It has been shown that the complex of ribosomal proteins prepared from various species of bacteria (8, 9), animals (3, 15), and higher plants (1,2,4,11,12,14) differ. Previous studies in our laboratory (5) employing two-dimensional electrophoresis to compare proteins of 70S and 80S wheat leaf ribosomes revealed that the proteins of chloroplast and cytoplasmic ribosomes differed in numbers, in their relative amounts, and in electrophoretic mobilities. The cytoplasmic ribosomes contained more proteins than have been reported for animals, and the chloroplast ribosomes contained more than have been reported for prokaryotes. Both classes of ribosomes contained a relatively large number of proteins that migrated towards the anode.In view of these findings, we set out to extend the work by comparing the ribosomal proteins of several species of higher plants. This report deals with the 80S cytoplasmic ribosomes of these species.MATERIALS AND METHODS Ribosomes from green leaves of different plant species were prepared by the method reported earlier (7). Leaves of 4.5-dayold seedlings of Triticum aestivum cv. Manitou, Triticum 'To whom reprint requests should be addressed. durum cv. Hercules, Hordeum vulgare cv. Gateway, Secale cereale cv. Prolific, and primary leaves of 10-day-old Phaseolus vulgaris cv. Black wax and Pisum sativum cv. Homesteader were used for isolation of the cytoplasmic ribosomes. Spinacia oleracea cv. Bloomsdale was supplied fresh by a local market gardener. For separation of 70S and 80S ribosomes from the same plant material in large quantities, a 7 to 35% (w/v) convex sucrose density gradient centrifugation was carried out in a Beckman Ti 14 zonal rotor (6). The Mg concentrations of the isolation media as well as of the zonal buffers were adjusted to provide optimal yield of ribosomes from the individual plant species. The concentrations were 1 mm for barley, 5 mM for beans, peas, and spinach, and 10 mm for rye and wheat.Proteins were extracted from the cytoplasmic ribosomes with 66% acetic acid in the presence of 30 mm MgClh. After lyophilization, the ribosomal proteins were dissolved in the electrophoresis buffer containing 6 M urea, and the protein concentration was determined by the method of Lowry et al. (10). For separation of the ribosomal proteins, the modified method of Ka...

show abstract

Section: Methodssupporting

confidence: 75%

Section: Methodsmentioning

confidence: 99%

mentioning

confidence: 93%

See 1 more Smart Citation

Comparison of Plant Cytoplasmic Ribosomal Proteins by Two-Dimensional Polyacrylamide Gel Electrophoresis

Nagabhushan

Gulyás²,

Zalik³

1974

Plant Physiol.

Self Cite

View full text Add to dashboard Cite

show abstract

“…Much (5)(6)(7)10). Two-dimensional acrylamide gel fractionation has been utilized in the study of cytoplasmic and chloroplast ribosomes of wheat (12).…”

mentioning

confidence: 99%