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ribonucleic acid/glycine max

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7 結果
The effects of the herbicide sethoxydim {2-[1-ethoxyimino)-butyl]-5-[2-(ethylthio)-propyl]-3-hydroxy-2-cyclohexen-1-one} on selected metabolic processes of enzymatically isolated leaf cells from soybeans [Glycine max (L.) Merr., cv. "Essex"] were studied. Photosynthesis, protein, ribonucleic acid

The occurrence and distribution of poly(a) ribonucleic Acid in soybean.

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The occurrence and distribution of poly(A) sequences in the RNA of soybean (Glycine max var. Wayne) have been studied. Only one of the two species of AMP-rich RNA contains poly(A). D-RNA does not contain detectable poly(A) sequences. The TB-RNA is the poly(A) RNA in this system. At least a part (up
An investigation has been made of the RNA synthesized by chromatin-bound RNA polymerase from soybean hypocotyls (Glycine max var. Wayne). Polymerase activity is 4- to 5-fold higher with chromatin from tissue treated with 2,4-dichlorophenoxyacetic acid, a synthetic auxin, compared to untreated
Two major peaks of RNA polymerase activity have been routinely separated by diethylaminoethyl cellulose chromatography following solubilization from soybean (Glycine max L. var. Wayne) chromatin. The relative amounts of these two peaks depend upon the manner in which the chromatin is purified.
The relative levels of multiple RNA polymerases were determined in soybean (Glycine max L. var. Wayne) hypocotyl during various stages of development. The meristematic region of the hypocotyl contains more total polymerase activity per gram fresh weight and a greater proportion of polymerase I
An effective method for the isolation of nucleoli from auxin-treated soybean (Glycine max, var. Wayne) hypocotyl was developed by polytron homogenization and sucrose gradient centrifugation. The nucleoli expressed only the alpha-amanitin-insensitive RNA synthetic activity. This activity
Concentrations of cycloheximide as low as 3 mug/ml inhibited incorporation of labeled orotic acid or uridine into RNA cytidylic acid of soybean (Glycine max) hypocotyl sections. Even lower concentrations of this well known protein synthesis inhibitor interfered with conversion of labeled cytidine
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