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Etheno-substituted nucleotides and coenzymes: fluorescence and biological activity.
  • N. Leonard
  • Biology, Medicine
  • CRC critical reviews in biochemistry
  • 1984
The binding of e-substituted nucleotides or polynucleotides to proteins has been determined for F- and G-actin, heavy meromyosin, tobacco mosaic virus protein, gene 32 protein of bacteriophage T4, and chloroplast... Expand
Cytokinins: Structure/activity relationships☆
Abstract Sixty-nine compounds, mostly purine derivatives and closely related substances, were tested for promotion of growth and regulation of organ formation in the tobacco bioassay to determineExpand
Adenosine cyclic 3',5'-monophosphate dependent protein kinase: a new fluorescence displacement titration technique for characterizing the nucleotide binding site on the catalytic subunit.
It is found that modifications of the adenine moiety reduce nucleotide affinity for the enzyme, and was most pronounced with modifications at position 6 of the base. Expand
Purification and characterization of the purE, purK, and purC gene products: identification of a previously unrecognized energy requirement in the purine biosynthetic pathway.
A new energy requirement in the purine biosynthetic pathway has been established and the gene products of the purE and purK genes thought to be responsible for this activity have been overexpressed and the proteins purified to homogeneity. Expand
Specificity of the 1-methyladenine receptors in starfish oocytes: synthesis and properties of some 1,8-disubstituted adenines, 1,6-dimethyl-1H-purine, and of the 1-(azidobenzyl)adenines
A selective synthesis of 1,6-dimethylpurine (16) and the preparations of the 1-(azidobenzyl)adenines (11)–(13), 8-azido-1-benzyladenine (10), and 1-methyladenine derivatives (2)–(9) with variousExpand
Isolation of cis-Zeatin from Corynebacterium fascians Cultures.
Three cytokinin-active constituents have been isolated from the culture medium of Corynebacterium fascians, a plant pathogen causing fasciation and one constituent is now identified as cis-zeatin, which represents the first unequivocal demonstration of the production of a zeatin isomer by a bacterial species. Expand