A Cytokinin-binding Protein from Wheat Germ
نویسندگان
چکیده
منابع مشابه
A Cytokinin-binding Protein from Wheat Germ: Isolation by Affinity Chromatography and Properties.
A cytokinin-binding protein has been isolated from wheat germ via ammonium sulfate precipitation, carboxymethyl Sephadex chromatography, and affinity chromatography on a column substituted with a derivative of kinetin riboside. On Sephadex G-200, the protein migrated with an apparent molecular weight of 122,000 daltons. The dissociation constant for kinetin was determined by equilibrium dialysi...
متن کاملMetabolism of cytokinin: deribosylation of cytokinin ribonucleoside by adenosine nucleosidase from wheat germ cells.
Adenosine nucleosidase (adenosine ribohydrolase, EC 3.2.2.7) which catalyzes the deribosylation of N(6)-(Delta(2)-isopentenyl)adenosine and adenosine to form the corresponding bases was partially purified from wheat germ. This enzyme (molecular weight 59,000 +/- 3,000) deribosylates the ribonucleosides at an optimum pH of 4.7 K(m) values for the cytokinin nucleoside and adenosine are 2.38 and 1...
متن کاملDistribution of Cytokinin-active Ribonucleosides in Wheat Germ tRNA Species.
The distribution of cytokinin activity in wheat (Triticum aestivum) germ tRNA fractionated by BD-cellulose and RPC-5 chromatography has been examined. As in other organisms, the cytokinin moieties in wheat germ tRNA appear to be restricted to tRNA species that would be expected to respond to codons beginning with U. Only a few of the wheat germ tRNA species in this coding group actually contain...
متن کاملHistone-specific protein-arginine methyltransferase from wheat germ.
Protein methylase I (S-adenosyl-L-methionine:protein (arginine) N-methyltransferase; EC 2.1.1.23) has been purified from wheat germ approximately 90-fold with a yield of 160%. This unusually high yield of the enzyme activity suggested the presence of an inhibitor. Subsequently, this inhibitor was purified to homogeneity and was found to be identical with adenosine; W absorption spectrum, retent...
متن کاملA fatty-acid-binding protein from wheat kernels.
A protein of about 7 kDa (W-FABP) has been isolated from mature wheat kernels by H2O extraction and gel filtration of the extract, followed by two steps of high-performance liquid chromatography. The N-terminal amino acid-sequence has been determined up to the 28th residue and found to be identical (except for positions 4 and 5) to that deduced from a barley cDNA (EMBL X15257), which had been i...
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ژورنال
عنوان ژورنال: Plant Physiology
سال: 1979
ISSN: 0032-0889,1532-2548
DOI: 10.1104/pp.64.4.594