Purification of leucine tRNA isoaccepting species from soybean cotyledons. II. RPC-2 [reversed phase chromatography] purification, ribosome binding, and cytokinin content

Two of the six leucine isoaccepting tRNA species from soybean (Glycine max) cotyledons recognize U-beginning codons, and contain cytokinin moieties in their structure. These same two isoaccepting species have been shown to undergo quantitative changes in their relative amounts upon treatment with N(...

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Published inPlant physiology (Bethesda) Vol. 63; no. 1; pp. 87 - 92
Main Authors Lester, B.R, Morris, R.O, Cherry, J.H
Format Journal Article
LanguageEnglish
Published United States 1979
Subjects
field crops
plant biochemistry
plant physiology
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Summary:Two of the six leucine isoaccepting tRNA species from soybean (Glycine max) cotyledons recognize U-beginning codons, and contain cytokinin moieties in their structure. These same two isoaccepting species have been shown to undergo quantitative changes in their relative amounts upon treatment with N(6)-benzyladenine in vivo. In addition a procedure has been developed for purification of the isoaccepting species of leucine tRNA from soybean cotyledons resulting in isoacceptors of minimum purity, calculated by amino acid acceptance capacity, of from 46 to 78% leucine tRNA.
Bibliography:F60
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To whom correspondence should be addressed.
Journal Paper No. 6633 of the Purdue Agricultural Experiment Station.
Present address: Department of Cell Biology, Baylor College of Medicine, Houston, Texas 77030.
Present address: Department of Agricultural Chemistry, Oregon State University, Corvallis, Oregon.
ISSN:0032-0889
1532-2548
DOI:10.1104/pp.63.1.87