The multicomponent analysis of estrogens in urine by ion exchange chromatography and GC-MS—I. Quantitation of estrogens after initial hydrolysis of conjugates

1987 ◽  
Vol 28 (2) ◽  
pp. 203-213 ◽  
Author(s):  
T. Fotsis ◽  
H. Adlercreutz
Keyword(s):  
Ion Exchange ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Multicomponent Analysis ◽  
Hydrolysis Of

scholarly journals PEMISAHAN ASAM AMINO DARI LIMBAH CAIR PABRIK KELAPA SAWIT DENGAN KROMATOGRAFI PENUKAR ION

2018 ◽  
Vol 6 (2) ◽  
pp. 69
Author(s):  
Indah Rahmi Sari ◽  
Ade Ayu Oksari ◽  
Irma Kresnawaty
Keyword(s):  
Amino Acid ◽  
Ion Exchange ◽  
Liquid Waste ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Enzyme Hydrolysis ◽  
Protease Enzyme ◽  
Absorbance Reading ◽  
Amino Acid Levels ◽  
Hydrolysis Of

Separation of Amino acid from Liquid waste of Oil palm Factory with Ion Exchange Chromatography Research on Separation of Amino Acid Liquid Waste mills with Ion Exchange Chromatography was carried out from October to November 2015. The results of  hydrolysis of 6 N HCl results showed  that the highest absorbance reading was obtained at a concentration of eluent of 0,2 and 0,6 M NaCl, while the results of the protease enzyme hydrolysis the highest absorbance reading at NaCl eluent 0,2 and 1 M. There was no significant difference in the results of separation by ion exchange chromatography, showed that the concentration of NaCl eluent is not very influential, so for subsequent analysis used only one concentration of the eluent. Results of linear regression obtained was equal to 0,9946, these results indicate that the series standard amino acid lysine has a value that is linear as it approaches 1. The amino acid levels obtained on the sample results LCPKS hydrolysis with 6 N HCl which was about 0 to 8.82 ppm and samples of the protease enzyme hydrolysis of about 0 to 4.31 ppm. Amino acid levels obtained were still far from the expected.Keywords: Amino Acid, Oil Palm, Liquid Waste, Ion Exchange Chromatography ABSTRAKPenelitian mengenai Pemisahan Asam Amino dari Limbah Cair Pabrik Kelapa Sawit dengan Kromatografi Penukar Ion telah dilaksanakan dari bulan Oktober sampai November 2015. Hasil hidrolisis HCl 6 N menunjukkan bahwa pembacaan absorbansi tertinggi diperoleh pada konsentrasi eluen NaCl 0,2 dan 0,6 M, sedangkan hasil hidrolisis enzim protease pembacaan absorbansi tertinggi pada eluen NaCl 0,2 dan 1 M. Tidak ada perbedaan yang signifikan pada hasil pemisahan dengan kromatografi penukar ion ini, menunjukkan bahwa konsentrasi eluen NaCl tidak terlalu berpengaruh, sehingga untuk analisis selanjutnya digunakan hanya satu konsentrasi eluen. Hasil regresi linear yang diperoleh yaitu sebesar 0,9946, hasil tersebut menunjukkan bahwa deret standar asam amino lisin mempunyai nilai yang linear karena mendekati 1. Kadar asam amino yang diperoleh pada sampel hasil hidrolisis LCPKS dengan HCl 6N yaitu sekitar 0 – 8,82 ppm dan sampel hasil hidrolisis enzim protease sekitar 0 – 4,31 ppm. Kadar asam amino yang diperoleh masih jauh dari yang diharapkan.Kata Kunci: Asam Amino, Minyak Kelapa Sawit, Limbah Cair, Kromatografi Penukar Ion

scholarly journals Preparation, purification and analyses of thirteen alkali-stable dinucleotides from ribonucleic acid

1970 ◽  
Vol 116 (4) ◽  
pp. 589-598 ◽  
Author(s):  
A. R. Trim ◽  
Janet E. Parker
Keyword(s):  
Nucleotide Sequence ◽  
Ion Exchange ◽  
Ribonucleic Acid ◽  
Deae Cellulose ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Spectroscopic Constants ◽  
Commercial Yeast ◽  
High Degree ◽  
Hydrolysis Of

Of the 16 alkali-stable dinucleotides known to be obtained by hydrolysis of commercial yeast RNA with alkali, 13 were prepared in quantities of the order of 10mg or more. The samples, with only one exception, contain at least 90% of dinucleotide, and spectroscopic constants and nucleotide-sequence determinations, although not conclusive, indicate a high degree of purity of these products. The small dinucleotide fraction in 150g of RNA hydrolysed with alkali (1–2% of the total nucleotides) was separated from the mononucleotides by stepwise ion-exchange chromatography on DEAE-cellulose columns and resolved into seven fractions containing from one to four different dinucleotides by electrophoresis on paper at pH3.0. These fractions were resolved into their constituent dinucleotides by chromatography in ammonium sulphate. Contamination of the products by impurities from the paper was minimized by washing it before using it for chromatography or electrophoresis and, by using a thick grade of paper (Whatman no. 17), it was possible to handle and purify relatively large quantities of nucleotides.

Early Stages of the Hydrolysis of Chromium(III) in Aqueous Solution. V. Measurement of the Equilibrium Between Singly and Doubly Bridged Dimer

1989 ◽  
Vol 42 (9) ◽  
pp. 1579 ◽  
Author(s):  
T Merakis ◽  
L Spiccia
Keyword(s):  
Aqueous Solution ◽  
Hydrogen Bonding ◽  
Ion Exchange ◽  
Dissociation Constant ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Acid Dissociation ◽  
Acid Dissociation Constant ◽  
Thermodynamic Constants ◽  
Hydrolysis Of

Ion-exchange chromatography has been used to measure the equilibrium between singly bridged (SBD) and doubly bridged (DBD) forms of the hydrolytic dimer of chromium(III), at variable [H+] (0.008-0.97 M) and T (288.2-318.2 K) and constant I (1.0 M). From these measurements, the acid dissociation constant, Kal , for SBD, and the equilibrium constant, K, for interconversion between monodeprotonated SBD and DBD have been determined together with their corresponding thermodynamic constants. The results at 298.2K were as follows: K = 10.1( �0.6) [ΔH� = -10( �3) kJ mol-1 and ΔS�=-15( �9) J K-1 mol-1]; KKal = 1 .83(�0.04) mol dm-3 [ΔS� = 30(�1) kJ mol-1 and ΔS�= 104(�4) J K-1 mol-1]; Kal = 0.18( �0.2) mol dm-3 [ΔS�= 43(�4) kJ mol-l and ΔS�= 128(�13) J K-1 mol-1]. The high Kalis attributed to the participation of monodeprotonated SBD in hydrogen bonding. As the temperature increases, the overall equilibrium (given by KKal ) is driven towards DBD by a dramatic increase in the acidity ( Kal ) of SBD, an increase which more than offsets a concurrent decrease in K.

Some properties of a highly thermostable α-amylase from a Thermoactinomyces sp.

1984 ◽  
Vol 30 (6) ◽  
pp. 780-785 ◽  
Author(s):  
S. K. C. Obi ◽  
F. J. C. Odibo
Keyword(s):  
Molecular Weight ◽  
Enzyme Activity ◽  
Ion Exchange ◽  
Gel Filtration ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Enzyme Activation ◽  
Cow Dung ◽  
C 30 ◽  
Hydrolysis Of

Thermostable α-amylase from Thermoactinomyces sp. No. 15, isolated from cow dung, was partially purified and characterized. The enzyme was purified (318-fold) by acetone precipitation, ion-exchange chromatography, and gel filtration techniques. The molecular weight was estimated to be 47 800. Optimum enzyme activity was recorded at pH 7 and at 80 °C. The enzyme was stable at pH 5.0–10.0 and retained 74% activity at 100 °C (30 min). Enzyme activation was observed in the presence of Mn2+, Ag+, and Fe2+, but Hg2+ and Zn2+ were inhibitory. Products of hydrolysis of native starches were mainly glucose and maltose.

Purification of extracellular amylolytic enzymes from the thermophilic fungus Thermomyces lanuginosus

1988 ◽  
Vol 34 (3) ◽  
pp. 218-223 ◽  
Author(s):  
Bo Jensen ◽  
Jorgen Olsen ◽  
Knud Allermann
Keyword(s):  
Molecular Weight ◽  
Ion Exchange ◽  
Soluble Starch ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Thermomyces Lanuginosus ◽  
Amylolytic Enzymes ◽  
Molecular Weights ◽  
Isoelectric Points ◽  
Hydrolysis Of

When grown in static culture it appears as if Thermomyces lanuginosus has a biphasic secretion of the extracellular starch-degrading activity. This could be due to the presence of at least two different amylases. By ion-exchange chromatography on DEAE-Trisacryl an α-amylase (EC 3.2.1.1) and a glucoamylase (EC 3.2.1.3) were separated and purified from the extracellular protein from 14-day-old static cultures grown on soluble starch. The hydrolysis of soluble starch by the purified glucoamylase resulted in only glucose as the end product, whereas the α-amylase gave maltose as the smallest end product. The molecular weights and isoelectric points of the enzymes were for glucoamylase 70 000 – 76 000 and pH 4.0, and for α-amylase 54 000 – 57 000 and pH 3.4. An α-glucosidase (EC 3.2.1.20) with a molecular weight of 44 000 – 48 000 and an isoelectric point at pH 3.8 was eluted close to the α-amylase fraction on the DEAE-Trisacryl column.

scholarly journals Inositol Phosphate Phosphatases of Microbiological Origin. Inositol Phosphate Intermediates in the Dephosphorylation of the Hexaphosphates of Myo-Inositol, Scyllo-Inositol, and D-Chiro-Inositol by a Bacterial (Pseudomonas sp.) Phytase

1970 ◽  
Vol 23 (5) ◽  
pp. 1207 ◽  
Author(s):  
DJ Cosgrove
Keyword(s):  
Ion Exchange ◽  
Inositol Phosphate ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Pseudomonas Sp ◽  
Inositol Hexaphosphate ◽  
Hydrolysis Of

Inositol phosphate n;termediates formed during the enzymic (bacterial phytase) dephosphorylation of the hexaphosphates of myo-, scyllo-, and D-chiroinositol have been isolated by means of ion-exchange chromatography. Hydrolysis of myo-inositol hexaphosphate is believed to proceed via D-myo-inositol 1,2,4,5,6- pentaphosphate, D-myo-inositol 1,2,5,6-tetraphosphate, D-myo-inositol 1,2,5- or 1,2,6-triphosphate or both, D-myo-inositol 1,2-diphosphate, and finally myoinositol 2-monophosphate.

MONOSACCHARIDE COMPOSITION OF SELECTED CANADIAN PEATS

1980 ◽  
Vol 60 (1) ◽  
pp. 1-7 ◽  
Author(s):  
H. MORITA ◽  
W. G. MONTGOMERY
Keyword(s):  
Liquid Chromatography ◽  
Ion Exchange ◽  
Acid Hydrolysis ◽  
Monosaccharide Composition ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Fibre Content ◽  
Gas Liquid Chromatography ◽  
Chemical Feature ◽  
Hydrolysis Of

The neutral monosaccharides released by the acid hydrolysis of five peat profiles were analyzed by ion exchange chromatography and gas-liquid chromatography in order to ascertain whether monosaccharide composition can be used to differentiate peats. Glucose, mannose and galactose were the predominant monosaccharides found. Changes observed with depth in the relative abundances of the monosaccharides were not always correlated with the degree of decomposition as measured by fibre content or pyrophosphate index. The arabinose to xylose ratio was a diagnostic chemical feature which reflected the degree of decomposition of the peats.

scholarly journals The location of N-acetylgalactosamine in the walls of Bacillus subtilis 168

1972 ◽  
Vol 130 (3) ◽  
pp. 691-696 ◽  
Author(s):  
M. Duckworth ◽  
A. R. Archibald ◽  
J. Baddiley
Keyword(s):  
Bacillus Subtilis ◽  
Ion Exchange ◽  
Growth Conditions ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Free Sugar ◽  
Bacillus Subtilis 168 ◽  
Hydrolysis Of

The N-acetylgalactosamine in the walls of Bacillus subtilis 168 occurs in two polymers. One of these contains N-acetylgalactosamine, glucose and phosphorus and is attached to the peptidoglycan through an alkali-labile bond; preliminary studies indicate that a repeating unit of this polymer is glucosyl-N-acetylgalactosamine 1-phosphate. N-Acetylgalactosamine is also associated with the peptidoglycan in a component that is not converted into the free sugar or other soluble compounds on treatment of the walls with alkali. The two polymers containing N-acetylgalactosamine are released on autolysis of the walls and can be separated by ion-exchange chromatography. As glucose 6-phosphate is produced by gentle hydrolysis of the wall with acid a third phosphate polymer, poly(glucose 1-phosphate), may occur in this wall. However, as no polymer with this structure could be separated from that containing galactosamine, its existence has not been established unequivocally. The methods described permit the study of variations in N-acetylgalactosamine content with respect to growth conditions.

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