منابع مشابه
Histone Kinase from Soybean Hypocotyls: PURIFICATION, PROPERTIES, AND SUBSTRATE SPECIFICITIES.
A histone-type protein kinase (EC 2.7.1.37) has been partially purified (320-fold) from the crude extracts of soybean hypocotyls by means of a combination of gel filtration and anion exchange procedures. The purified enzyme fraction is devoid of the activities of phosphoprotein phosphatase (EC 3.1.3.16), histone protease, and casein (or phosvitin)-type kinase. The soybean histone kinase uses AT...
متن کاملPhosphoprotein Phosphatase of Soybean Hypocotyls: PURIFICATION, PROPERTIES, AND SUBSTRATE SPECIFICITIES .
A soybean histone-type protein kinase was used to prepare (32)P-labeled histone H1 as substrate for purification and characterization of a phosphoprotein phosphatase (EC 3.1.3.16) from soybean hypocotyls. The phosphatase has been purified 169-fold by ammonium sulfate fractionation, ethanol precipitation, and chromatography on Sephadex G-150, DEAE-Sephadex A-25 and Sephadex G-100. The activity o...
متن کاملMetabolic Regulation during Glyceollin Biosynthesis in Green Soybean Hypocotyls.
The accumulation of the isoflavonoid phytoalexin, glyceollin, occurs in hypocotyls of green soybean seedlings (Glycine max L. Merr. cv Harosoy 63) in response to the injection of a glucan elicitor isolated from the mycelial walls of the fungus, Phytophthora megasperma f. sp. glycinea. This accumulation, which levels off after 24 hours, is preceded by a dramatic, transient rise in extractable ac...
متن کاملAssociation of Phytochrome with Rough-surfaced Endoplasmic Reticulum Fractions from Soybean Hypocotyls.
Distribution of phytochrome (as Pfr) among membranes from soybean hypocotyls (Glycine max L. cv. Wayne) was determined by the combined techniques of cell fractionation, difference spectrometry, and electron microscopic morphometry. More than 90% of the phytochrome was found in the soluble fraction. With homogenates prepared in the presence or absence of Mg(2+), the portion associated with membr...
متن کاملPurification and characterization of arginine decarboxylase from soybean (Glycine max) hypocotyls.
Arginine decarboxylase (EC 4.1.1.19) was purified from soybean, Glycine max, hypocotyls by a procedure which includes ammonium sulfate fractionation, acetone precipitation, gel filtration chromatography, and affinity chromatography. Using this procedure, ADC was purified to one band in non-denaturing PAGE. The purified ADC has an M(r) of 240 kDa based on gel filtration chromatography and is a t...
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ژورنال
عنوان ژورنال: Plant Physiology
سال: 1980
ISSN: 0032-0889,1532-2548
DOI: 10.1104/pp.66.3.360