FRACTIONATION AND DISSOCIATION OF THE AVIAN LIPOVITELLINS AND THEIR INTERACTION WITH PHOSVITIN

1964 ◽  
Vol 42 (3) ◽  
pp. 395-406 ◽  
Author(s):  
M. W. Radomski ◽  
W. H. Cook
Keyword(s):  
Ionic Strength ◽  
Phosphate Buffer ◽  
Structural Changes ◽  
Phosphorus Content ◽  
Egg Yolk ◽  
Gradient Elution ◽  
Progressive Change ◽  
Hen’S Egg ◽  
Dowex 1 ◽  
Elution Chromatography

Phosvitin and lipovitellin, the granule proteins of hen's egg yolk, were clearly separated by gradient elution on Dowex-1 columns. No phosvitin could be detected in the lipovitellin fraction but the first eluates of the phosvitin fraction contained lipovitellin of high protein phosphorus content. These initial eluates contained only two components sedimenting at rates slightly higher than dimer and monomer lipovitellin. As the lipovitellin monomer does not ordinarily occur in neutral solvents, the slower sedimenting material is either a new component or the monomer stabilized through interaction with phosvitin.Gradient elution chromatography of the total lipovitellins on hydroxyapatite showed that β-lipovitellin was completely eluted by 0.6 M phosphate buffer at pH 6.8 and appeared to be homogeneous. However, α-lipovitellin was heterogeneous: it was eluted over a concentration range of 0.7 to 1.4 M and the protein phosphorus content and dissociative behavior of successive fractions showed a progressive change with increasing ionic strength. Superimposed on this general heterogeneity of α-lipovitellin, there was consistent evidence of two poorly defined components, and three when the α-fraction was rechromatographed. Following dissociation and reassociation, there was no evidence of hybridization between monomers of α- and β-lipovitellin. Changes in the chromatographic patterns of α-lipovitellin following dissociation may indicate hybridization of different α-monomers, but these could also arise from structural changes in the monomers.

Gradient Elution Chromatography of the Acids in Concord and Other Grape Juices and Jellies

1965 ◽  
Vol 48 (3) ◽  
pp. 534-543
Author(s):  
David Jorysch ◽  
Seymour Marcus
Keyword(s):  
Citric Acid ◽  
Exchange Resin ◽  
Anion Exchange Resin ◽  
Free Acid ◽  
Grape Juice ◽  
Gradient Elution ◽  
Fraction Collector ◽  
Grape Juices ◽  
Dowex 1 ◽  
Elution Chromatography

Abstract The gradient elution technique was used to determine the acid profiles of grape juices and jellies prepared from their juices. Acids were separated by placing predetermined volumes of grape juices containing equal milliequivalents of free acid on columns of Dowex 1-X10 anion exchange resin in the formate form and eluting with formic acid in gradually increasing concentration. The eluates were collected in a fraction collector and evaporated to dryness on a waterbath, and the residues were titrated with standard alkali solution. The gradient elution chromatograms of the acids in Concord grape juice samples pressed in the laboratory differed only slightly from similar commercial samples. Grape juices other than Concord have similar acid patterns but show another acid peak. Grape jellies were liquefied and their acids determined by the method; the presence of added citric acid in these jellies is shown to affect the acidity patterns.

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.

CHROMATOGRAPHIC SEPARATION OF PHOSVITIN, α- AND β-LIPOVITELLIN OF EGG YOLK GRANULES ON TEAE-CELLULOSE

1964 ◽  
Vol 42 (8) ◽  
pp. 1203-1215 ◽  
Author(s):  
M. W. Radomski ◽  
W. H. Cook
Keyword(s):  
Ionic Strength ◽  
Egg Yolk ◽  
Gradient Elution ◽  
Partial Recovery ◽  
Linear Gradient ◽  
Yolk Granules ◽  
Sedimentation Behavior ◽  
Strength Limit ◽  
The Individual ◽  
Low Ionic Strength

The two components of lipovitellin and the three major components of yolk granules, phosvitin, α- and β-lipovitellin, have been separated by gradient elution chromatography on TEAE-cellulose. A 0.2 M phosphate buffer (pH 6.8) had the necessary ionic strength to dissolve these proteins and when applied in this solvent all components except β-lipovitellin were retained by the column. A linear gradient of ionic strength (limit buffer 0.2 M phosphate plus 0.5 M NaCl) was used to remove the other components. Recovery was essentially complete and the composition and properties of the individual components were similar to those obtained by previous chromatographic methods that gave only partial recovery. An additional component eluted after α-lipovitellin and before phosvitin, previously observed in Dowex-1 separations, was also observed by the present method. The composition, sedimentation behavior, and absorption spectra of this component indicate that it is a soluble complex of phosvitin and lipovitellin. When granules are dissolved in alkaline solvents (pH 9.4) of low ionic strength (0.05), phosvitin is not evident as a separate component during ultracentrifugation, but appears as the ionic strength is increased.

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.

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.

scholarly journals Distinct Structural Changes Detected by X-Ray Fiber Diffraction in Stabilization of F-Actin by Lowering pH and Increasing Ionic Strength

2001 ◽  
Vol 80 (2) ◽  
pp. 841-851 ◽  
Author(s):  
Toshiro Oda ◽  
Kouji Makino ◽  
Ichiro Yamashita ◽  
Keiichi Namba ◽  
Yuichiro Maéda
Keyword(s):  
Ionic Strength ◽  
Structural Changes ◽  
X Ray ◽  
Fiber Diffraction

Biological characteristics of an enterotoxin produced by Bacillus cereus

1975 ◽  
Vol 21 (8) ◽  
pp. 1236-1246 ◽  
Author(s):  
W. M. Spira ◽  
J. M. Goepfert
Keyword(s):  
Ionic Strength ◽  
Bacillus Cereus ◽  
Exponential Growth ◽  
Biological Activities ◽  
Egg Yolk ◽  
Immune Serum ◽  
Fluid Accumulation ◽  
Ileal Loop ◽  
Receptor Sites ◽  
Ph Range

An enterotoxin synthesized during exponential growth by Bacillus cereus produces fluid accumulation in rabbit ileal loops, alters vascular permeability in the skin of rabbits, and kills mice when injected intravenously. All activities are eluted simultaneously from a Sephadex G-75 column and are distinct from the hemolysin and egg yolk turbidity factor of B. cereus. The enterotoxin is a true exotoxin. It interacts with intestinal receptor sites in a highly transient manner in the ileal loop system. Rabbit immune serum produced against the culture fluids from one strain of B. cereus neutralized the three biological activities in all other strains tested except strain B-6-ac for which none of the activities were neutralized.Enterotoxin proved to be unstable under a wide variety of conditions; ionic strength was especially critical. Enterotoxin was most stable in a pH range of 5.0 to 10.0, but lost activity rapidly outside this range. Alkylation provided some protection of enterotoxin activity in crude preparations but failed to protect activity during purification procedures. It did not appear to affect critically the enterotoxin molecule itself, since elution profiles on Sephadex G-75 chromatography were unchanged after alkylation.

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