form
saline suspension
extent of labeling
2-10 μmol per mL
matrix
Cross-linked 4% beaded agarose
matrix activation
cyanogen bromide
matrix attachment
amino
matrix spacer
1 atom
storage temp.
2-8°C
Application
L-Phenylalanine-agarose is used in protein chromatography, affinity chromatography and amino acid resins. L-Phenylalanine-agarose has been used to purify and characterize a cysteine protease of Fasciola gigantica adult worms as well as to purify a proteolytic enzyme of the liver fluke Fasciola species.
Physical form
Suspension in 2.0 M NaCl containing preservative
Storage Class
12 - Non Combustible Liquids
wgk_germany
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
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T Aoki et al.
Molecular and biochemical parasitology, 8(2), 89-97 (1983-06-01)
A proteolytic enzyme of the liver fluke Fasciola sp. was purified as described previously by ammonium sulfate fractionation, gel filtration on Sephadex G-200 column and L-phenylalanine-agarose chromatography. Leupeptin, a peptide aldehyde of microbial origin, competitively inhibited the enzyme activity with
J F Geissler et al.
Journal of bacteriology, 170(4), 1709-1714 (1988-04-01)
A soluble benzoate-coenzyme A (CoA) ligase was purified from the phototrophic bacterium Rhodopseudomonas palustris. Synthesis of the enzyme was induced when cells were grown anaerobically in light with benzoate as the sole carbon source. Purification by chromatography successively on hydroxylapatite
K H Lau et al.
The Journal of biological chemistry, 260(8), 4653-4660 (1985-04-25)
A partially purified bovine cortical bone acid phosphatase, which shared similar characteristics with a class of acid phosphatase known as tartrate-resistant acid phosphatase, was found to dephosphorylate phosphotyrosine and phosphotyrosyl proteins, with little activity toward other phosphoamino acids or phosphoseryl
B O Fagbemi et al.
Veterinary parasitology, 43(3-4), 223-232 (1992-07-01)
A 26-28 kDa protease was isolated from Fasciola gigantica adult worms by a two-stage purification process of column chromatography in a Sephacryl S-200 column and affinity chromatography in an L-phenylalanine-agarose column. This protease is a cysteine (thiol) proteinase with an
H R Onishi et al.
The Journal of biological chemistry, 254(23), 11943-11952 (1979-12-10)
The nonspecific alkaline phosphatase of yeast (Saccharomyces strain 1710) has been purified by ion exchange, hydrophobic, and affinity chromatography. This vacuolar enzyme has a molecular weight of 130,000 and is composed of subunits (probably of 66,000 molecular weight). It also
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