Results 1 to 10 of about 756 (126)

Enhanced Analysis of Low-Abundance Proteins in Soybean Seeds Using Advanced Mass Spectrometry. [PDF]

open access: yesInt J Mol Sci
Meng B   +10 more
europepmc   +1 more source

Genomic Insights into Cyanide Biodegradation in the Pseudomonas Genus. [PDF]

open access: yesInt J Mol Sci
Sáez LP   +6 more
europepmc   +1 more source

The one-carbon metabolic enzyme MTHFD2 promotes resection and homologous recombination after ionizing radiation. [PDF]

open access: yesMol Oncol
Marttila P   +14 more
europepmc   +1 more source

Development of Potent and Selective Inhibitors of Methylenetetrahydrofolate Dehydrogenase 2 for Targeting Acute Myeloid Leukemia: SAR, Structural Insights, and Biological Characterization. [PDF]

open access: yesJ Med Chem
Chang HH   +19 more
europepmc   +1 more source
Some of the next articles are maybe not open access.

Characterization of purified guanine aminohydrolase

Archives of Biochemistry and Biophysics, 1979
Abstract Guanine aminohydrolase (GAH) (E.C. 3.5.4.3) was purified by affinity chromatography on 9-( p -β-aminoethoxyphenyl)guanine-Sepharose to a specific activity of 35.5 units/mg. The molecular weight of the enzyme was estimated to be 110,000 by gel filtration.
J D, Bergstrom, A L, Bieber
openaire   +2 more sources

On the regulatory properties of deoxycytidylate aminohydrolase

Biochemical and Biophysical Research Communications, 1964
Abstract In a previous paper we suggested the occurrence of at least one regulatory site ( Scarano et al., 1962 , Scarano et al., 1963 ) on dCMP aminohydrolase. The present paper reports further experiments that support this hypothesis.
E, Scarano, G, Geraci, M, Rossi
openaire   +2 more sources

Characterization of bovine liver guanine aminohydrolase

International Journal of Biochemistry, 1981
Abstract 1. 1. The isoelectric points of bovine liver guanine aminohydrolase and xanthine oxidase are 4.90 and 6.25, respectively. 2. 2. The molecular weight of the guanine aminohydrolase is 95,000. 3. 3. The guanine aminohydrolase is formed from two subunits of identical molecular weight.
J M, Galilea, E I, Canela, J, Bozal
openaire   +2 more sources

A fluorimetric assay for guanine aminohydrolase

Analytical Biochemistry, 1974
Abstract A rapid, sensitive, and versatile assay for guanine aminohydrolase is described. It is based on the difference in native fluorescence of guanine, the substrate, and xanthine, the reaction product when excitation and emission wavelengths are 285 nm and 345 nm, respectively.
openaire   +2 more sources

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