scholarly journals The Gel Filtration Chromatographic-Profiles of Proteins and Peptides of Wort and Beer: Effects of Processing - Malting, Mashing, Kettle Boiling, Fermentation and Filtering

2003 ◽  
Vol 109 (1) ◽  
pp. 41-50 ◽  
Author(s):  
A.M. Osman ◽  
S.M. Coverdale ◽  
K. Onley-Watson ◽  
D. Bell ◽  
P. Healy
Keyword(s):  
Gel Filtration ◽  
Chromatographic Profiles ◽  
Proteins And Peptides

scholarly journals Proteomic characterization of two snake venoms: Naja naja atra and Agkistrodon halys

2004 ◽  
Vol 384 (1) ◽  
pp. 119-127 ◽  
Author(s):  
Shuting LI ◽  
Jingqiang WANG ◽  
Xumin ZHANG ◽  
Yan REN ◽  
Ning WANG ◽  
...  
Keyword(s):  
Southern China ◽  
Gel Filtration ◽  
Complex Mixture ◽  
Tandem Ms ◽  
Post Translational Modification ◽  
Combination Strategy ◽  
Naja Naja ◽  
Maldi Tof ◽  
Proteins And Peptides ◽  
Naja Atra

Snake venom is a complex mixture of proteins and peptides, and a number of studies have described the biological properties of several venomous proteins. Nevertheless, a complete proteomic profile of venom from any of the many species of snake is not available. Proteomics now makes it possible to globally identify proteins from a complex mixture. To assess the venom proteomic profiles from Naja naja atra and Agkistrodon halys, snakes common to southern China, we used a combination strategy, which included the following four different approaches: (i) shotgun digestion plus HPLC with ion-trap tandem MS, (ii) one-dimensional SDS/PAGE plus HPLC with tandem MS, (iii) gel filtration plus HPLC with tandem MS and (iv) gel filtration and 2DE (two-dimensional gel electrophoresis) plus MALDI–TOF (matrix-assisted laser desorption ionization–time-of-flight) MS. In the present paper, we report the novel identification of 124 and 74 proteins and peptides in cobra and viper venom respectively. Functional analysis based upon toxin categories reveals that, as expected, cobra venom has a high abundance of cardio- and neurotoxins, whereas viper venom contains a significant amount of haemotoxins and metalloproteinases. Although approx. 80% of gel spots from 2DE displayed high-quality MALDI-TOF-MS spectra, only 50% of these spots were confirmed to be venom proteins, which is more than likely to be a result of incomplete protein databases. Interestingly, these data suggest that post-translational modification may be a significant characteristic of venomous proteins.

scholarly journals Chromatographic Profiles of Umami Fractions from Indonesian Commercial Salty Soy Sauce

2020 ◽  
Vol 16 (2) ◽  
pp. 36
Author(s):  
Hanifah Nuryani Lioe ◽  
Diana Ayu Nindita ◽  
Warsono El Kiyat
Keyword(s):  
Gel Filtration ◽  
Soy Sauce ◽  
Gel Filtration Chromatography ◽  
Hplc Chromatogram ◽  
Rp Hplc ◽  
Hplc Profiles ◽  
Taste Dilution Analysis ◽  
Chromatographic Profiles

Salty soy sauce subjected in this study is a variety of commercial soy products in Indonesia. Chromatographic profiles linked to taste dilution analysis of the soy sauce were analyzed by Sephadex G-15 gel filtration chromatography followed by RP-HPLC. The results showed that there were 4 umami fractions (Fractions I − IV) obtained by Sephadex G-15 separation. Chromatographic profiles at 254 nm could show the differentiation of the four fractions and then their RP-HPLC profiles were proven to be different from each other. Fraction III which contained 65% of the soy sauce dry matters, had the highest umami intensity with umami TD factor of 256, meanwhile, this fraction was tasted salty due to the salt contained in the soy sauce. Fraction III was dominated by the later peaks in the RP-HPLC chromatogram, which was more hydrophobic. The hydrophobic components were commonly tasted bitter, perhaps in the commercial salty soy sauce, the taste interaction between the umami and bitter components might have occurred.

Characteristics of Superdex® prep grade media for gel filtration chromatography of proteins and peptides

1996 ◽  
Vol 31 (2) ◽  
pp. 163-172 ◽  
Author(s):  
Ulf Hellberg ◽  
Jöns-Petter Ivarsson ◽  
Bo-Lennart Johansson
Keyword(s):  
Gel Filtration ◽  
Gel Filtration Chromatography ◽  
Proteins And Peptides

Acid-Ethanol Extractable Compounds from Fruits and Seeds of the Bitter Gourd Momordica Charantia: Effects on Lipid Metabolism in Isolated Rat Adipocytes

1987 ◽  
Vol 15 (01n02) ◽  
pp. 31-42 ◽  
Author(s):  
T.B. Ng ◽  
C.M. Wong ◽  
W.W. Li ◽  
H.W. Yeung
Keyword(s):  
Lipid Metabolism ◽  
Gel Filtration ◽  
Momordica Charantia ◽  
Bitter Gourd ◽  
Rat Adipocytes ◽  
Glucose Incorporation ◽  
P Fraction ◽  
Extractable Compounds ◽  
Isolated Rat ◽  
Proteins And Peptides

Fruits and seeds of the bitter gourd Momordica charantia (Family Cucurbitaceae) were extracted with the acidic ethanol. The extract was adjusted to pH 3 and proteins and peptides were precipitated by additon of a copious volume of aceton. The precipitate was dissolved, dialyzed and lyophilized. The resulting material, designated "p-fraction" was tested for antilipolytic and lipogenic activities. Seed "p-fraction" was further chromatographed on fetuin agraose to yield an unadsorbed fraction (F) which could be fractioned by gel filtration on Sephadex G-10 to give an unretarted fraction (F1) and a retarted function (F2). Fruit "p-fraction" exhibited antilipolytic activity in hamster adipocytes and stimulated 3H-glucose incorporation into lipids, F1, a saponin containing fraction, inhibited both lipolysis and 3H-glucose incorporation into lipids. F2 enhance 3H-glucose corporation into lipid. The results are indicavie of the presence of compounds with insulinomimetic activities in M. charantia fruits and seeds.

scholarly journals Use of α-Lactalbumin [α-La] from Whey as a Vehicle for Bioactive Compounds in Food Technology and Pharmaceutics: A Review

2021 ◽  
Vol 03 (02) ◽  
pp. 1-1
Author(s):  
Andrea P. Cuevas-Gómez ◽  
◽  
Izlia J. Arroyo-Maya ◽  
Humberto Hernández-Sánchez ◽  
◽  
...  
Keyword(s):  
Whey Protein ◽  
Food Industry ◽  
Membrane Separation ◽  
Gel Filtration ◽  
Filtration Membrane ◽  
Production Technologies ◽  
Pharmaceutical Industries ◽  
Mineral Binding ◽  
Whey Protein Isolates ◽  
Proteins And Peptides

Whey protein is a byproduct of cheese, casein, and Greek yogurt produced in Europe, North America, and Australasia. It is a substantial source of functional proteins and peptides for the worldwide food industry. α-Lactalbumin (α-La) is a globular protein that can be isolated from WPI (whey protein isolates) using techniques such as chromatography/gel filtration, membrane separation, etc. α-La is used in the elaboration of functional foods and is a very good source of peptides with anticancer, antimicrobial, antiviral, antihypertensive, immunomodulating, opioid, mineral-binding, and antioxidant bioactivities. Nanotubes and nanoparticles generated from this protein are utilized as vehicles for the transport of active compounds, and thus, can be used in foods and pharmaceutical industries. The contaminant effects of whey, characteristics of α-La, production technologies, and its applications in nanotechnology are reviewed here.

Fluorescent Substances in Protein Hydrolysates. II. Comparison of Some Protein and Peptide Hydrolysates

1971 ◽  
Vol 49 (1) ◽  
pp. 6-11 ◽  
Author(s):  
M. Ledvina ◽  
F. S. LaBella
Keyword(s):  
Amino Acid ◽  
Acid Hydrolysis ◽  
Degradation Products ◽  
Gel Filtration ◽  
Fluorescence Emission ◽  
Fluorescent Products ◽  
Tryptophan Content ◽  
Tryptophan Derivatives ◽  
Fluorescent Derivatives ◽  
Proteins And Peptides

Fluorescence was measured in the hydrolysates of several proteins and peptides of known amino acid composition. The most intense fluorescence (emission maximum at 445 nm) was found in acid, but not enzymic, hydrolysates of tryptophan-rich proteins; nine fluorescent fractions were resolved from acid hydrolysates of these proteins by gel filtration. Fluorescence of substances in tryptophan-containing proteins is largely eliminated by reduction, but little affected by oxidation or ultraviolet irradiation. The substances are thermostable and apparently are not amino acids.Tyrosine, tyrosine-containing peptides, and tryptophan-free proteins yielded fewer fluorescent products than did tryptophan-rich proteins. The number and amount of fluorescent derivatives produced from tyrosine during acid hydrolysis depends on the particular protein; also, intra- or intermolecular interactions involving tyrosine or its degradation products appear to influence the nature of fluorescence in protein hydrolysates.The present findings suggest possible quantitation of the tryptophan content of proteins by fluorometric measurement of tryptophan derivatives produced by acid hydrolysis.

A quantitative gel-filtration method for analysis of the proteinaceous fraction of Cheddar cheese

1974 ◽  
Vol 41 (2) ◽  
pp. 259-268 ◽  
Author(s):  
P. M. D. Foster ◽  
Margaret L. Green
Keyword(s):  
Gel Filtration ◽  
Molecular Size ◽  
Solvent System ◽  
Main Peak ◽  
Filtration Method ◽  
The Third ◽  
Small Peak ◽  
Cheese Curd ◽  
A Minor ◽  
Proteins And Peptides

SummaryMethods are described for the solubilization of the nitrogenous portion of cheese in a dissociating solvent system and separation of the solution into fractions on a Sephadex G-100 column under conditions where the proteins and peptides would be expected to be split into monomeric units. TheE280measurement of the fractions, expressed as a percentage of the total material eluted, followed a reproducible pattern, both with duplicate runs on the same sample and comparative runs on non-identical samples of the same type. With cheese curd, a small peak of undissociated material was obtained at the void volume of the column; this was followed by a main peak and a minor third peak, with a small quantity of material being eluted at larger volumes. A qualitatively similar pattern was obtained with 43-day-old cheese as the sample, but the main peak was smaller, the third peak was larger, and a relatively larger amount of material was eluted at greater volumes. There was only partial separation of the proteins on the column; the main peak contained β- and αs-caseins, their larger breakdown products and some para-κ-casein, and the third peak contained smaller breakdown products of the main casein fractions and para-κ-casein. Although the resolution was considerably inferior to that obtained by gel electrophoresis, the method has the advantage over this and other methods in that it gives a quantitative analysis of the sample based on molecular size. Thus, it is suggested that it may find use in analysing protein breakdown in cheese during ripening.

Immunocytochemical Localization of Amyloid Protein AA in the “Dense Fibrillar Inclusions” of the Reticuloendothelical Cells

1977 ◽  
Vol 35 ◽  
pp. 438-439
Author(s):  
T. Shirahama ◽  
M. Skinner ◽  
A.S. Cohen
Keyword(s):  
Amyloid Fibril ◽  
Close Association ◽  
Gel Filtration ◽  
Fibril Formation ◽  
Amyloid Protein ◽  
Electron Microscopic ◽  
Amyloid Deposits ◽  
Amyloid Fibril Formation ◽  
Electron Microscopic Technique ◽  
Lysosomal System

A1thought the mechanisms of amyloidogenesis have not been entirely clarified, proteolysis of the parent proteins may be one of the important steps in the amyloid fibril formation. Recently, we reported that "dense fibrillar inclusions" (DFI), which had the characteristics of lysosomes and contained organized fibrillar profiles as well, were observed in the reticuloendothelial cells in close association with the foci of new amyloid deposits. We considered the findings as evidence for the involvement of lysosomal system in amyloid fibril formation (l). In the present study, we attempted to determine the identity of the contents of the DFI by the use of antisera against the amyloid protein (AA) and an immuno-electron microscopic technique.Amyloidosis was induced in CBA/J mice by daily injections of casein (l). AA was isolated from amyloid-laden spleens by gel filtration and antibody to it was produced in rabbits (2). For immunocytochemistry, the unlabeled antibody enzyme method (3) was employed.

Sign in / Sign up

Export Citation Format

Share Document