The Experts below are selected from a list of 161262 Experts worldwide ranked by ideXlab platform
M.p.c. Da Silva - One of the best experts on this subject based on the ideXlab platform.
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Determination of the molecular weight distribution of hydroxyethylcellulose by Gel Filtration chromatography
Carbohydrate Polymers, 1995Co-Authors: John F. Kennedy, Z. S. Rivera, Linda L. Lloyd, F. P. Warner, M.p.c. Da SilvaAbstract:Abstract Due to the importance of the knowledge of the molecular weight distribution of hydroxyethylcellulose, (HEC), in predicting its performance, a study on the use of Gel Filtration chromatography for the determination of this information has been carried out. Results presented demonstrate that it is possible to use Gel Filtration columns with 100% aqueous eluents for the size separation and Gel Filtration analysis of a representative selection of water-soluble HEC samples. Data obtained correlate with the viscosity grading supplied with the samples by the manufacturer.
K. Datsyshyn - One of the best experts on this subject based on the ideXlab platform.
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Obtaining Of β-Lactoglobulin By Gel Filtration Of Cow Milk Whey
EUREKA: Life Sciences, 2019Co-Authors: V. Yukalo, K. Datsyshyn, Liudmyla StorozhAbstract:Milk whey proteins carry out a number of important biological functions and also they are precursors of many biologically active peptides (antihypertensive peptides, antagonists of opioid receptors, regulators of intestinal motility, immunomodulatory, anti-microbial and anti-cancer peptides, appetite regulators and so on.). An important stage in natural bioactive peptides obtaining from milk whey proteins is the isolation of homogeneous proteins-precursors. Considering the significant difference in the molecular masses of whey proteins, a promising method for their selection is Gel Filtration. The purpose of the research was the fractionation of bioactive peptides precursors from milk whey using Gel Filtration on Sephadex G-150. The whey was obtained from fresh skimmed milk after isoelectric precipitation of casein. Gel Filtration was carried out on the columns from a liquid chromatography kit by the “Reanal” company. The fractional composition and the degree of homogeneity of milk whey proteins were determined by disc-electrophoresis in the plates of a polyacrylamide Gel. A repeated Gel Filtration of fractions from the chromatographic peaks, separated into sections, was performed to increase the fractionation efficiency. While choosing a dextran Gel for Gel Filtration of precursors of biologically active peptides from milk whey proteins, we have taken into account the range of their molecular weights (from 10000 to 150000 Da), the ability to form supramolecular structures (β-LG), as well as the previously obtained results of Gel Filtration. As a result, it was shown that repeated Gel Filtration of milk whey on Sephadex G-150 allows efficiently fractionate the proteins-precursors of bioactive peptides. The range of peptides and proteins molecular weights that can be fractionated on this Sephadex is from 5000 to 300 000 Da. The usage of repeated Gel Filtration on Sephadex G-150 with the chromatogram separation into sectors allows to effectively fractionate proteins-precursors of bioactive peptides from milk whey. In particular, homogeneous β-lactoglobulin (degree of homogeneity > 95 %) and partially purified α-lactalbumin, as well as a group of immunoglobulins and a proteose-peptone fraction were obtained.
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Gel Filtration OF COW MILK WHEY PROTEINS
Food Science and Technology, 2019Co-Authors: V. Yukalo, K. DatsyshynAbstract:The work considers the isolation of homogeneous precursor proteins of biologically active peptides from milk whey by Gel Filtration, in conditions that maximally ensure the preservation of their structure, composition, and properties. Considering the range of molecular masses of the main precursor proteins, the sephadex G-100 was selected for the Gel Filtration. As a result of the Gel Filtration of milk whey on a column with this sephadex, three peaks have been obtained, one of which was asymmetric and divided into two sectors. In total, four sectors from the three peaks have been received. Further, an electrophoretic analysis in the polyacrylamide Gel of the proteins composition of all sectors was carried out. Sector A (the first peak) included immunoglobulins, lactoferrin, serum albumin. Sectors B and C (the second peak) consisted of β-lactoglobulin and α-lactalbumin in different ratios. The components of sector D (the third peak) had a small molecular weight and did not contain proteins. The next stage of the work was obtaining homogeneous lactoproteins. To this end, another Gel Filtration of the combined fractions of sectors A, B, and C was performed. Each of the chromatographic peaks obtained was divided into three ranges for the analysis of the proteins composition. Analytical electrophoresis of the combined chromatographic fractions of each range has shown that in six ranges out of nine, homogeneous precursor proteins of bioactive peptides were present. As a result of this repeated Gel Filtration on sephadex G-100, two homogeneous fractions (β-lactoglobulin, immunoglobulins) were obtained, which together, based on the results of the three Gel Filtrations, composed 59% of the whole milk whey protein. The processing of electrophoregrams, with the use of the image reading function imread, has shown high homogeneity of the fractions obtained (immunoglobulins ˃ 90%, and β-lactoglobulin ˃94%). These fractions were used to develop a biotechnology for obtaining and studying bioactive antihypertensive and bactericidal peptides from milk whey proteins.
V. Yukalo - One of the best experts on this subject based on the ideXlab platform.
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Obtaining Of β-Lactoglobulin By Gel Filtration Of Cow Milk Whey
EUREKA: Life Sciences, 2019Co-Authors: V. Yukalo, K. Datsyshyn, Liudmyla StorozhAbstract:Milk whey proteins carry out a number of important biological functions and also they are precursors of many biologically active peptides (antihypertensive peptides, antagonists of opioid receptors, regulators of intestinal motility, immunomodulatory, anti-microbial and anti-cancer peptides, appetite regulators and so on.). An important stage in natural bioactive peptides obtaining from milk whey proteins is the isolation of homogeneous proteins-precursors. Considering the significant difference in the molecular masses of whey proteins, a promising method for their selection is Gel Filtration. The purpose of the research was the fractionation of bioactive peptides precursors from milk whey using Gel Filtration on Sephadex G-150. The whey was obtained from fresh skimmed milk after isoelectric precipitation of casein. Gel Filtration was carried out on the columns from a liquid chromatography kit by the “Reanal” company. The fractional composition and the degree of homogeneity of milk whey proteins were determined by disc-electrophoresis in the plates of a polyacrylamide Gel. A repeated Gel Filtration of fractions from the chromatographic peaks, separated into sections, was performed to increase the fractionation efficiency. While choosing a dextran Gel for Gel Filtration of precursors of biologically active peptides from milk whey proteins, we have taken into account the range of their molecular weights (from 10000 to 150000 Da), the ability to form supramolecular structures (β-LG), as well as the previously obtained results of Gel Filtration. As a result, it was shown that repeated Gel Filtration of milk whey on Sephadex G-150 allows efficiently fractionate the proteins-precursors of bioactive peptides. The range of peptides and proteins molecular weights that can be fractionated on this Sephadex is from 5000 to 300 000 Da. The usage of repeated Gel Filtration on Sephadex G-150 with the chromatogram separation into sectors allows to effectively fractionate proteins-precursors of bioactive peptides from milk whey. In particular, homogeneous β-lactoglobulin (degree of homogeneity > 95 %) and partially purified α-lactalbumin, as well as a group of immunoglobulins and a proteose-peptone fraction were obtained.
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Gel Filtration OF COW MILK WHEY PROTEINS
Food Science and Technology, 2019Co-Authors: V. Yukalo, K. DatsyshynAbstract:The work considers the isolation of homogeneous precursor proteins of biologically active peptides from milk whey by Gel Filtration, in conditions that maximally ensure the preservation of their structure, composition, and properties. Considering the range of molecular masses of the main precursor proteins, the sephadex G-100 was selected for the Gel Filtration. As a result of the Gel Filtration of milk whey on a column with this sephadex, three peaks have been obtained, one of which was asymmetric and divided into two sectors. In total, four sectors from the three peaks have been received. Further, an electrophoretic analysis in the polyacrylamide Gel of the proteins composition of all sectors was carried out. Sector A (the first peak) included immunoglobulins, lactoferrin, serum albumin. Sectors B and C (the second peak) consisted of β-lactoglobulin and α-lactalbumin in different ratios. The components of sector D (the third peak) had a small molecular weight and did not contain proteins. The next stage of the work was obtaining homogeneous lactoproteins. To this end, another Gel Filtration of the combined fractions of sectors A, B, and C was performed. Each of the chromatographic peaks obtained was divided into three ranges for the analysis of the proteins composition. Analytical electrophoresis of the combined chromatographic fractions of each range has shown that in six ranges out of nine, homogeneous precursor proteins of bioactive peptides were present. As a result of this repeated Gel Filtration on sephadex G-100, two homogeneous fractions (β-lactoglobulin, immunoglobulins) were obtained, which together, based on the results of the three Gel Filtrations, composed 59% of the whole milk whey protein. The processing of electrophoregrams, with the use of the image reading function imread, has shown high homogeneity of the fractions obtained (immunoglobulins ˃ 90%, and β-lactoglobulin ˃94%). These fractions were used to develop a biotechnology for obtaining and studying bioactive antihypertensive and bactericidal peptides from milk whey proteins.
John F. Kennedy - One of the best experts on this subject based on the ideXlab platform.
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Determination of the molecular weight distribution of hydroxyethylcellulose by Gel Filtration chromatography
Carbohydrate Polymers, 1995Co-Authors: John F. Kennedy, Z. S. Rivera, Linda L. Lloyd, F. P. Warner, M.p.c. Da SilvaAbstract:Abstract Due to the importance of the knowledge of the molecular weight distribution of hydroxyethylcellulose, (HEC), in predicting its performance, a study on the use of Gel Filtration chromatography for the determination of this information has been carried out. Results presented demonstrate that it is possible to use Gel Filtration columns with 100% aqueous eluents for the size separation and Gel Filtration analysis of a representative selection of water-soluble HEC samples. Data obtained correlate with the viscosity grading supplied with the samples by the manufacturer.
Liudmyla Storozh - One of the best experts on this subject based on the ideXlab platform.
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Obtaining Of β-Lactoglobulin By Gel Filtration Of Cow Milk Whey
EUREKA: Life Sciences, 2019Co-Authors: V. Yukalo, K. Datsyshyn, Liudmyla StorozhAbstract:Milk whey proteins carry out a number of important biological functions and also they are precursors of many biologically active peptides (antihypertensive peptides, antagonists of opioid receptors, regulators of intestinal motility, immunomodulatory, anti-microbial and anti-cancer peptides, appetite regulators and so on.). An important stage in natural bioactive peptides obtaining from milk whey proteins is the isolation of homogeneous proteins-precursors. Considering the significant difference in the molecular masses of whey proteins, a promising method for their selection is Gel Filtration. The purpose of the research was the fractionation of bioactive peptides precursors from milk whey using Gel Filtration on Sephadex G-150. The whey was obtained from fresh skimmed milk after isoelectric precipitation of casein. Gel Filtration was carried out on the columns from a liquid chromatography kit by the “Reanal” company. The fractional composition and the degree of homogeneity of milk whey proteins were determined by disc-electrophoresis in the plates of a polyacrylamide Gel. A repeated Gel Filtration of fractions from the chromatographic peaks, separated into sections, was performed to increase the fractionation efficiency. While choosing a dextran Gel for Gel Filtration of precursors of biologically active peptides from milk whey proteins, we have taken into account the range of their molecular weights (from 10000 to 150000 Da), the ability to form supramolecular structures (β-LG), as well as the previously obtained results of Gel Filtration. As a result, it was shown that repeated Gel Filtration of milk whey on Sephadex G-150 allows efficiently fractionate the proteins-precursors of bioactive peptides. The range of peptides and proteins molecular weights that can be fractionated on this Sephadex is from 5000 to 300 000 Da. The usage of repeated Gel Filtration on Sephadex G-150 with the chromatogram separation into sectors allows to effectively fractionate proteins-precursors of bioactive peptides from milk whey. In particular, homogeneous β-lactoglobulin (degree of homogeneity > 95 %) and partially purified α-lactalbumin, as well as a group of immunoglobulins and a proteose-peptone fraction were obtained.
