Abstract
Incubation of etiolated 'Phaseolus vulgaris' coleoptiles shows a converse flux between soluble protein and reducing sugar. The rate of incorporation of radioactive arginine into protein was higher than that of radioactive leucine. Radioactive arginine incorporation into protein was linear up to 120 min and then started to decline. The rate of incorporation of radioactive leucine was increased by preincubation of the tissue in the incubation medium. Roots were found to contain more soluble protein and much less reducing sugar than the coleoptile. The optimum pH value for protein synthesis in coleoptile sections was found to be 6 for control tissues and 4 for those treated with 10-/sup 3/M IAA. This high concentration of IAA was also found to inhibit soluble protein synthesis, the incorporation rate of radioactive arginine and leucine into protein fraction, the secretion of hydrogen ion into the incubation medium and elongation of the bean segment. Kinetin at 2x10/sup -4/M and putrescine at 5mM both decreased the rate of /sup 14/C-arginine incorporation into soluble protein, but for /sup 14/C-leucine, this rate of incorporation was found to be increased after 90 min incubation with a preincubation of 30 min. In general, the change pattern of the soluble protein content,
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Citation Formats
Crocomo, O J, and Lee, T S.G.
Effects of putrescine, kinetin and IAA on protein synthesis in 'Phaseolus vulgaris' coleoptiles.
Brazil: N. p.,
1975.
Web.
Crocomo, O J, & Lee, T S.G.
Effects of putrescine, kinetin and IAA on protein synthesis in 'Phaseolus vulgaris' coleoptiles.
Brazil.
Crocomo, O J, and Lee, T S.G.
1975.
"Effects of putrescine, kinetin and IAA on protein synthesis in 'Phaseolus vulgaris' coleoptiles."
Brazil.
@misc{etde_6743982,
title = {Effects of putrescine, kinetin and IAA on protein synthesis in 'Phaseolus vulgaris' coleoptiles}
author = {Crocomo, O J, and Lee, T S.G.}
abstractNote = {Incubation of etiolated 'Phaseolus vulgaris' coleoptiles shows a converse flux between soluble protein and reducing sugar. The rate of incorporation of radioactive arginine into protein was higher than that of radioactive leucine. Radioactive arginine incorporation into protein was linear up to 120 min and then started to decline. The rate of incorporation of radioactive leucine was increased by preincubation of the tissue in the incubation medium. Roots were found to contain more soluble protein and much less reducing sugar than the coleoptile. The optimum pH value for protein synthesis in coleoptile sections was found to be 6 for control tissues and 4 for those treated with 10-/sup 3/M IAA. This high concentration of IAA was also found to inhibit soluble protein synthesis, the incorporation rate of radioactive arginine and leucine into protein fraction, the secretion of hydrogen ion into the incubation medium and elongation of the bean segment. Kinetin at 2x10/sup -4/M and putrescine at 5mM both decreased the rate of /sup 14/C-arginine incorporation into soluble protein, but for /sup 14/C-leucine, this rate of incorporation was found to be increased after 90 min incubation with a preincubation of 30 min. In general, the change pattern of the soluble protein content, the reducing sugar level and the incorporation rate of radioactive arginine and leucine into protein in the kinetin and putrescine treated tissues were about the same although tissues that incubated with kinetin always contain more soluble protein and less reducing sugar than that of incubated with putrescine.}
journal = []
volume = {18:1}
journal type = {AC}
place = {Brazil}
year = {1975}
month = {Jan}
}
title = {Effects of putrescine, kinetin and IAA on protein synthesis in 'Phaseolus vulgaris' coleoptiles}
author = {Crocomo, O J, and Lee, T S.G.}
abstractNote = {Incubation of etiolated 'Phaseolus vulgaris' coleoptiles shows a converse flux between soluble protein and reducing sugar. The rate of incorporation of radioactive arginine into protein was higher than that of radioactive leucine. Radioactive arginine incorporation into protein was linear up to 120 min and then started to decline. The rate of incorporation of radioactive leucine was increased by preincubation of the tissue in the incubation medium. Roots were found to contain more soluble protein and much less reducing sugar than the coleoptile. The optimum pH value for protein synthesis in coleoptile sections was found to be 6 for control tissues and 4 for those treated with 10-/sup 3/M IAA. This high concentration of IAA was also found to inhibit soluble protein synthesis, the incorporation rate of radioactive arginine and leucine into protein fraction, the secretion of hydrogen ion into the incubation medium and elongation of the bean segment. Kinetin at 2x10/sup -4/M and putrescine at 5mM both decreased the rate of /sup 14/C-arginine incorporation into soluble protein, but for /sup 14/C-leucine, this rate of incorporation was found to be increased after 90 min incubation with a preincubation of 30 min. In general, the change pattern of the soluble protein content, the reducing sugar level and the incorporation rate of radioactive arginine and leucine into protein in the kinetin and putrescine treated tissues were about the same although tissues that incubated with kinetin always contain more soluble protein and less reducing sugar than that of incubated with putrescine.}
journal = []
volume = {18:1}
journal type = {AC}
place = {Brazil}
year = {1975}
month = {Jan}
}