scholarly journals The isolation and composition of two phosphoproteins from hen's egg

1970 ◽  
Vol 118 (3) ◽  
pp. 537-542 ◽  
Author(s):  
R. C. Clark
Keyword(s):  
Molecular Weight ◽  
Minor Component ◽  
Egg Yolk ◽  
Terminal Residue ◽  
Hen’S Egg

1. Phosvitin extracted from domestic hen's-egg yolk was resolved on Sephadex G-100 into two phosphoprotein components. 2. The major component has a molecular weight of about 3.4×104 and alanine as an N-terminal residue. Glucosamine is present, but tyrosine is virtually absent. 3. The minor component has a molecular weight of about 2.8×104 and lysine as an N-terminal residue. Missing residues are glucosamine, methionine and leucine. Lysine, histidine, threonine, glycine, phenylalanine and tyrosine contents differ significantly from those of the major component. 4. Sephadex G-100 also removes small amounts of an impurity with a much higher molecular weight.

ISOLATION AND COMPOSITION OF AVIAN EGG YOLK GRANULES AND THEIR CONSTITUENT α- AND β-LIPOVITELLINS

1961 ◽  
Vol 39 (8) ◽  
pp. 1295-1307 ◽  
Author(s):  
R. W. Burley ◽  
W. H. Cook
Keyword(s):  
Molecular Weight ◽  
Low Temperature ◽  
Phosphorus Content ◽  
Low Density Lipoprotein ◽  
Density Lipoprotein ◽  
Egg Yolk ◽  
Low Density ◽  
High Molecular Weight Complex ◽  
Yolk Granules ◽  
Hen’S Egg

The yolk granules from hen's egg represent on a dry basis 23% of the yolk solids, and they contain about 90% of the protein phosphorus, 95% of the iron, and nearly 70% of the calcium in yolk. Ultracentrifugal and other analyses on solutions of the granules show that they are 70% α- and β-lipovitellin in an approximate ratio of 1:1.8, 16% phosvitin, and 12% low-density lipoprotein. The properties and composition of the two lipovitellins isolated from the granules are the same as those isolated from solutions of whole yolk. Further purification reduces the protein phosphorus in α-lipovitellin to 0.50% and in β-lipovitellin to 0.27%, and this confirms that α-vitellin has a higher phosphorus content. Experiments at low temperature suggest that phosvitin exists in the granules as a high molecular weight complex.

scholarly journals Two Low-molecular-weight Apoproteins (Apovitellenins I and II) from a Lipoprotein of Goose?s Egg Yolk: A Comparison with Related Species

1982 ◽  
Vol 35 (3) ◽  
pp. 263 ◽  
Author(s):  
AS Inglis ◽  
PM Strike ◽  
RW Burley
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Gel Filtration ◽  
Egg Yolk ◽  
Avian Species ◽  
Pekin Duck ◽  
Muscovy Duck ◽  
Hen’S Egg ◽  
Avian Family

As part of a comparative study of egg yolk from different avian species, the major lipoprotein and its mixed apoproteins from the egg yolk of the chinese goose (Anser cygnoides) have been prepared. From the apoprotein mixture, two new proteins, of molecular weight approximately 10000 and 22000 according to gel electrophoresis in detergent, have been isolated by gel-filtration chromato-graphy in urea. The protein of lower molecular weight corresponds in amino acid sequence to apovitellenin I, a protein previously isolated from other avian species. As a comparison with other members of the same avian family (Anatidae), the amino acid sequence of apovitellenin I from the pekin duck (Anas platyrhynchos) was re-investigated and that of the muscovy duck (Cairina moschata) investigated. These were found to be identical to the sequence of goose's apovitellenin I. The second new protein is similar in composition, molecular weight, and solubility to apovitellenin II, a protein present in small amount in hen's egg yolk. A protein corresponding to apovitellenin II could not, however, be detected in the egg yolk of either species of duck.

ULTRACENTRIFUGAL ANALYSIS OF YOLK PROTEINS IN RAINBOW TROUT EGG AND THEIR CHANGES DURING DEVELOPMENT

1965 ◽  
Vol 43 (3) ◽  
pp. 373-379 ◽  
Author(s):  
Kazuo Ando
Keyword(s):  
Molecular Weight ◽  
Rainbow Trout ◽  
Phosphorus Content ◽  
Sedimentation Coefficient ◽  
Egg Yolk ◽  
Yolk Proteins ◽  
Hen’S Egg ◽  
Synchronous Development ◽  
Protein Components ◽  
Ultracentrifugal Analysis

Yolk proteins in Salmo irideus (rainbow trout) eggs were studied by means of ultracentrifugal analysis, and the following facts were clarified. Unfertilized eggs contain two protein components, designated as component I (90% in relative content) and component II (10%). The sedimentation constant for component I is 9.4 S and its molecular weight is approximately 240,000 ~ 260,000. The phosphorus and lipid contents of this major component are similar to those of a lipovitellin in hen's egg yolk, but the molecular weight is considerably smaller than that of the hen's lipovitellin. Component I is split by alkali into two subunits. The sedimentation coefficient for the subunits is 4.9 S and the molecular weight is approximately 120,000. The sedimentation coefficient for component II is 3.1 S, and the phosphorus content is higher than that of component I but is lower than that of hen's phosvitin. A new component of 11.2 S appears at the beginning of the eyed stage, and is inferred to be a protein in the blood formed at this stage. The relative changes of these three components during the synchronous development of embryo from fertilization to the swim-up fry stage were followed.

scholarly journals Studies on the Apoproteins of the Major Lipoprotein of the Yolk of Hen's Eggs. IV. Aggregation in Urea of Proteins of Intermediate and High Molecular Weight and the Isolation of Four Electrophoretically Distinct Proteins

1980 ◽  
Vol 33 (3) ◽  
pp. 255 ◽  
Author(s):  
RW Burley ◽  
RW Sleigh
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Gel Filtration ◽  
Egg Yolk ◽  
Gel Filtration Chromatography ◽  
Hen’S Egg

The gel-filtration chromatography of the total apoprotein mixture from hen's egg yolk lipoprotein in acidic 6 M urea has been re-examined using the gel-filtration materials Sephadex and cross-linked Sepharose. Electrophoresis has also been used in attempts at separating the constituents of intermediate and high molecular weight.

A COMPARISON OF PHOSVITINS PREPARED FROM HEN'S SERUM AND FROM HEN'S EGG YOLK

1961 ◽  
Vol 39 (1) ◽  
pp. 109-117 ◽  
Author(s):  
Chi-Ching Mok ◽  
W. G. Martin ◽  
R. H. Common
Keyword(s):  
Molecular Weight ◽  
Average Molecular Weight ◽  
Egg Yolk ◽  
Terminal Amino Acid ◽  
Weight Average Molecular Weight ◽  
Sedimentation Constant ◽  
Hen’S Egg ◽  
Zone Electrophoresis ◽  
Terminal Amino ◽  
Tryptophan Content

A phosvitin has been prepared from the serum of estrogenized laying hens and partially characterized on the basis of its contents of N (12.3%), P (10.1%), serine (31.0%), and tryptophan (0.56%). Examination of this serum phosvitin and a yolk phosvitin preparation for N-terminal groups yielded identical chromatographic patterns. Alanine was the major N-terminal amino acid with minor amounts of N-terminal lysine. The sedimentation constant [Formula: see text], weight-average molecular weight 4.2 × 104(Archibald method), and number-average molecular weight 4.0 × 104(calculated from the tryptophan content) of the serum phosvitin were similar to those of the phosvitin prepared from egg yolk by the same preparative technique. The two preparations behaved similarly when subjected to zone electrophoresis on paper.Zone electrophoretic evidence is submitted for the presence of phosvitin in the supernatant from dilution precipitation of crude lipophosphoprotein from laying hen's serum as well as in the precipitate itself.

6,8-Dihydroxypurine in the Hen’s Egg Yolk

1973 ◽  
Vol 28 (7-8) ◽  
pp. 482-483
Author(s):  
S. De Boeck ◽  
T. Rymen ◽  
J. Stockx
Keyword(s):  
Egg Yolk ◽  
Hen’S Egg

Characterization of glycopeptides derived from the low-density lipoprotein of hen's egg yolk

1968 ◽  
Vol 46 (8) ◽  
pp. 983-988 ◽  
Author(s):  
J. Z. Augustyniak ◽  
W. G. Martin
Keyword(s):  
Low Density Lipoprotein ◽  
Density Lipoprotein ◽  
Egg Yolk ◽  
Low Density ◽  
Amide Nitrogen ◽  
Acetylneuraminic Acid ◽  
Hen’S Egg ◽  
Terminal Amino ◽  
Protein Moiety

Two glycopeptides (A and B) were isolated from pronase-digested vitellenin, the protein moiety of the low-density lipoprotein of hen's egg yolk. Aspartic acid was the only N-terminal amino acid of both glycopeptides but only A contained N-acetylneuraminic acid. A contained 55% hexose (mannose), 14% hexosamine, 12% N-acetylneuraminic acid, 0.71% amide nitrogen, and its molecular weight was 2.3 × 103. The corresponding values for B were 64, 17, 0.0, 0.75, and 2.0 × 103. Chemical analyses showed that B (and probably A) occurs in vitellenin with the heteropolysaccharide group bound N-glycosidically via the β-amide group of an asparaginyl residue. The indicated structure is R∙(NH)Asp∙Thr∙Ser∙(Ala, Gly, Val)∙Ile, where R, the heteropolysaccharide group, contains 2 hexosamine and 8 hexose residues.

Zinc- and copper-binding proteins in the plasma of winter flounder (Pseudopleuronectes americanus)

1980 ◽  
Vol 58 (4) ◽  
pp. 609-613 ◽  
Author(s):  
P. E. Fletcher ◽  
G. L. Fletcher
Keyword(s):  
Molecular Weight ◽  
Binding Proteins ◽  
Binding Protein ◽  
Gel Filtration ◽  
Protein S ◽  
Egg Yolk ◽  
Winter Flounder ◽  
Zinc Binding ◽  
Copper Binding ◽  
Copper Binding Proteins

Zinc- and copper-binding proteins were isolated from the plasma of winter flounder using gel filtration chromatography. A single copper-binding protein fraction of molecular weight 170 000 was isolated from the plasma of both sexes.In male and female flounder over 95% of the plasma zinc was associated with a zinc-binding protein(s) with a molecular weight of 76 000. In male flounder the remaining zinc appeared to be bound to a protein(s) of molecular weight 186 000. In female flounder the remaining 5% of the zinc was associated with two zinc-binding fractions with apparent molecular weights of 186 000 and 340 000 – 370 000.Extracts of plasma vitellogenin and egg yolk proteins revealed significant quantities of zinc and copper. It is hypothesized that the female specific zinc-binding protein (340 000 – 370 000) was vitellogenin.

scholarly journals Rat liver alcohol dehydrogenase. Purification and properties

1971 ◽  
Vol 125 (4) ◽  
pp. 1039-1047 ◽  
Author(s):  
M J Arslanian ◽  
E Pascoe ◽  
J G Reinhold
Keyword(s):  
Molecular Weight ◽  
Alcohol Dehydrogenase ◽  
Rat Liver ◽  
Gel Filtration ◽  
Rabbit Antiserum ◽  
Minor Component ◽  
Disc Electrophoresis ◽  
Supernatant Fraction ◽  
Liver Alcohol Dehydrogenase ◽  
A Minor

Alcohol dehydrogenase (EC 1.1.1.1) from the rat liver supernatant fraction has been purified 200-fold and partially characterized. The isolation procedure involved ammonium sulphate fractionation, DEAE-Sephadex chromatography and gel filtration. The purified enzyme behaved as a homogeneous preparation as evaluated by cellulose acetate and polyacrylamide-gel disc electrophoresis. Sulphoethyl-Sephadex chromatography and immunoelectrophoresis with rabbit antiserum indicated the presence of a minor component. Rat liver alcohol dehydrogenase appears to contain 4mol of zinc/mol, has an estimated molecular weight of 65000 and consists of two subunits of similar molecular weight. Heavy-metal ions, thiol-blocking reagents, urea at concentrations below 8m, low pH (5.5) and chelating agents deactivate the enzyme but do not dissociate it into subunits. Deactivated enzyme could not be reactivated. The enzyme is strictly specific for NAD+ and has a broad specificity for alcohols, which are bound at a hydrophobic site. Inhibition occurred with the enzyme equilibrated with Zn2+ at concentrations above 0.1mm.

Isolation of Immunoglobulin from Chicken Egg Yolk using Single-Stage Ultrafiltration with 100-kDa Regenerated Cellulose Membranes

2011 ◽  
Vol 7 (1) ◽  
Author(s):  
Jianguo Liu ◽  
Juan Yang ◽  
Hai Xu ◽  
Hu Zhu ◽  
Jianbo Qu ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Egg Yolk ◽  
Single Stage ◽  
Regenerated Cellulose ◽  
Cellulose Membrane ◽  
Permeate Flux ◽  
Operational Parameters ◽  
Solution Ph ◽  
Chicken Egg ◽  
Chicken Egg Yolk

The aim of this work is to develop a membrane-based cost-effective process for the rapid isolation of immunoglobulin from chicken egg yolk. It was found that a single-stage ultrafiltration using a 100 kDa molecular weight cut-off regenerated cellulose membrane could be employed to isolate immunoglobulin from the crude feedstock. The effects of operational parameters (solution pH, ionic strength, stirring speed and permeate flux) on the transmission of immunoglobulin and the presence of impurity protein with molecular weight close to immunoglobulin were quantified using the parameter scanning ultrafiltration technique. Under optimized conditions, the purity of immunoglobulin obtained was about 85 percent after the single-stage ultrafiltration process, and the recovery of immunoglobulin from the feedstock was 91 percent.

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