scholarly journals Comparison of Similar Protein Components Isolated from Wool and Wool Roots

1966 ◽  
Vol 19 (4) ◽  
pp. 699 ◽  
Author(s):  
R Frater
Keyword(s):  
Amino Acid ◽  
Gel Electrophoresis ◽  
Deae Cellulose ◽  
Protein Composition ◽  
Starch Gel Electrophoresis ◽  
Starch Gel ◽  
Protein Components ◽  
Derivatives Of ◽  
Peptide Maps ◽  
Root Proteins

Soluble derivatives of wool and wool-root proteins have been extracted by reduction with mercaptoethanol in the presence of 8M urea followed by alkylation with acrylonitrile. Using chromatography on DEAE-cellulose, followed by gelfiltration on Sephadex, one of the major low-sulphur proteins present in the extract has been isolated in a pure state as determined by starch-gel electrophoresis. Such pure proteins were isolated from extracts of wool and wool roots taken from the same animal. Proteins from these two sources were then compared on the basis of amino acid composition and peptide maps prepared from tryptic digests of them. The results show that small but significant differences do exist between the wool and wool-root proteins. Oomparisons of the protein from different wools show that differences also occur here. It is concluded that small changes must occur in the protein composition during the keratinization process.

scholarly journals Studies on Reduced Wool V. A Comparison of the Two Major Components

1965 ◽  
Vol 18 (6) ◽  
pp. 1207 ◽  
Author(s):  
EOP Thompson ◽  
IJ O'donnell
Keyword(s):  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Deae Cellulose ◽  
Major Protein ◽  
Starch Gel Electrophoresis ◽  
Starch Gel ◽  
Protein Components ◽  
Wool Proteins ◽  
Peptide Maps

Starch-gel electrophoresis of wool proteins extracted from reduced and carboxymethylated wool gives a complex pattern in which there are two major protein bands. By a combination of chromatography on DEAE-cellulose and gelfiltration in buffers containing 8M urea these two protein components have been isolated. The amino acid composition and some properties of these two fractions are reported. A comparison of the amino acid composition and of peptide maps of tryptic digests of the two fractions shows distinct differences between them, and by labelling with 2-[14C]iodoacetate the distribution of the peptides containing S-carboxymethylcysteine residues were also shown to be different.

scholarly journals Studies on Reduced Wool

1964 ◽  
Vol 17 (4) ◽  
pp. 973 ◽  
Author(s):  
IJ O'donnell ◽  
EOP Thompson
Keyword(s):  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Gel Electrophoresis ◽  
Deae Cellulose ◽  
Single Component ◽  
Starch Gel Electrophoresis ◽  
Starch Gel ◽  
Wool Proteins

Starch-gel electrophoresis in buffers containing 8ror urea has been used to follow the fractionation of wool proteins extracted from reduced and carboxy-methylated wool. Fractionation on both DEAE-cellulose and Sephadex G-200 in the presence of buffers containing Sr.t: urea is possible but in neither case is a single component obtained. However, a combination of these two methods has enabled one of the major components to be isolated. The amino acid composition of this material is reported.

scholarly journals A chromatographic preparation of ox growth hormone

1966 ◽  
Vol 100 (3) ◽  
pp. 593-600 ◽  
Author(s):  
M Wallis ◽  
HBF Dixon
Keyword(s):  
Molecular Weight ◽  
Growth Hormone ◽  
Gel Electrophoresis ◽  
Anterior Pituitary ◽  
Gel Filtration ◽  
Deae Cellulose ◽  
Starch Gel Electrophoresis ◽  
Highly Active ◽  
Cross Linkage ◽  
Starch Gel

1. A method is described for the chromatographic preparation of ox growth hormone. It involves chromatography of an extract of anterior pituitary lobes on DEAE-cellulose, followed by rechromatography on a dextran gel of low cross-linkage (Sephadex G-100). 2. The product is highly active in growth-hormone assays, and is obtained in good yield. It was homogeneous by several criteria, but showed some heterogeneity on starch-gel electrophoresis. 3. The molecular weight of the hormone was estimated from its behaviour on gel-filtration columns under various conditions. Evidence that the hormone may dissociate into sub-units under some conditions is presented.

scholarly journals Starch-Gel Electrophoresis of Wheat Flour Proteins

1963 ◽  
Vol 16 (2) ◽  
pp. 342 ◽  
Author(s):  
Janet SD Graham
Keyword(s):  
Acetic Acid ◽  
Wheat Flour ◽  
Gel Electrophoresis ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Starch Gel Electrophoresis ◽  
Similar Protein ◽  
Starch Gel ◽  
Protein Components ◽  
Electrophoresis Of Proteins

An improved apparatus and procedures for starch-gel electrophoresis of proteins of wheat flour are described; highly reproducible separation of the protein components was achieved. By starch-gel electrophoresis it was shown that similar protein components occur in the extracts of wheat flour obtained with a variety of solvents; however, there were marked differences in the proportions of these components in various extracts. Several protein components were present in the fJ'actions separated by ion-exchange chromatography of' the proteins soluble in Bodium pyrophosphate and of those soluble in acetic acid; some fractions containeda number of similar protein components.

STUDIES ON PLASMINOGEN: IV. ALTERATION OF BOVINE AND HUMAN PLASMINOGENS DURING ISOLATION

1966 ◽  
Vol 44 (4) ◽  
pp. 469-473 ◽  
Author(s):  
John Y. S. Chan ◽  
Edwin T. Mertz
Keyword(s):  
Ionic Strength ◽  
Gel Electrophoresis ◽  
Deae Cellulose ◽  
Starch Gel Electrophoresis ◽  
Major Band ◽  
Starch Gel ◽  
Human Plasminogen

Bovine and human plasminogen preparations were analyzed by starch-gel electrophoresis at pH 2.5 and 0.10 ionic strength. The bands were activated with urokinase and the proteolytic and esterolytic activities measured. Bovine euglobulin contains one plasminogen band, B-1. Plasminogen prepared from bovine euglobulin by continuous electrophoresis at pH 3.5 contains B-1 and a faster plasminogen band, B-2. B-1 and B-2 are also found in bovine plasminogen prepared by DEAE-cellulose chromatography. All three preparations on activation give the same two plasmin bands on starch gel. Human euglobulin also contains two active plasminogen bands H-1 and H-2. Plasminogen prepared from human euglobulin by continuous electrophoresis at pH 3.5 contains H-1, H-2, and a faster minor plasminogen band, H-3. All highly purified human plasminogens derived from Cohn fraction III contain either H-3 as a major band and an additional plasminogen band, H-4, or only H-3, but no H-1 and H-2. On activation with urokinase or streptokinase, human plasminogen preparations give one or two plasmin bands. It is concluded that bovine B-2 and human H-3 and H-4 are altered forms of euglobulin plasminogen created during isolation procedures. Essentially pure human H-3 can be prepared by continuous electrophoresis from Cutter plasminogen.

The Separation of Insect Haemolymph Proteins

1964 ◽  
Vol 96 (1-2) ◽  
pp. 110-110
Author(s):  
B. G. Loughton ◽  
P. Rueffel ◽  
H. Stich ◽  
A. S. West
Keyword(s):  
Amino Acid ◽  
Gel Electrophoresis ◽  
Starch Gel Electrophoresis ◽  
Homologous Proteins ◽  
Agar Gel ◽  
Diffusion Technique ◽  
Starch Gel ◽  
Rapid Characterization ◽  
Gel Diffusion

It has been suggested that information on the phylogenetic relationships of genera and species could be obtained by comparing the amino acid sequence in the homologous proteins of different species. This procedure is extremely difficult and time-consuming.However, a relatively rapid characterization of proteins can be obtained by analysing their mobilities with starch-gel electrophoresis and examination of antigenic diversity by the agar gel diffusion technique of Ouchterlony.

Benzylamine oxidase and histaminase: purification and crystallization of an enzyme from pig plasma

1964 ◽  
Vol 161 (983) ◽  
pp. 153-167 ◽  
Keyword(s):  
Ammonium Sulphate ◽  
Gel Electrophoresis ◽  
Copper Content ◽  
Deae Cellulose ◽  
Starch Gel Electrophoresis ◽  
Anaerobic Conditions ◽  
Concentrated Solutions ◽  
Radioactivation Analysis ◽  
Starch Gel ◽  
Benzylamine Oxidase

The enzyme benzylamine oxidase of pig plasma has been purified and some of the properties of the pure preparation have been studied. The purification procedure included several precipitations with ammonium sulphate and separations of proteins by column chromatography, first on DEAE-cellulose, followed by DEAE-Sephadex and lastly on a hydroxyapatite column. Crystals were prepared from solutions of the purified enzyme by adding ammonium sulphate. The crystalline preparation was homogeneous when studied by starch-gel electrophoresis and by ultracentrifugation. The molecular weight, as determined on the analytical ultracentrifuge, was 195 000. The copper content of the enzyme, as determined by radioactivation analysis, was about four atoms of Cu per molecule of enzyme. Concentrated solutions of the enzyme had a pink colour; the colour disappeared when substrate (benzylamine) was added under anaerobic conditions. The amines which were tested and found to be oxidized by the pure enzyme were: benzylamine, histamine, mescaline and 4-picolylamine. The affinity of the enzyme for benzylamine was more than one hundred times that for histamine.

scholarly journals The Amino Acid Composition of Hemoglobin. III. A Qualitative Method for Identifying Abnormalities of the Polypeptide Chains of Hemoglobin

Blood ◽  
1964 ◽  
Vol 24 (6) ◽  
pp. 750-756 ◽  
Author(s):  
AMOZ I. CHERNOFF ◽  
NELSON M. PETTIT
Keyword(s):  
Amino Acid ◽  
Amino Acid Composition ◽  
Gel Electrophoresis ◽  
Qualitative Method ◽  
Polypeptide Chain ◽  
Starch Gel Electrophoresis ◽  
Simple Method ◽  
Starch Gel ◽  
Barbital Buffer ◽  
Polypeptide Chains

Abstract A relatively simple method is described which permits the identification of abnormalities of either polypeptide chain of hemoglobin. The procedure is based on the dissociation of hemoglobin by 6 molar urea and starch-gel electrophoresis in a barbital buffer at pH 8.0.

Hemoglobin Mahidol: a new hemoglobin α-chain mutant

1970 ◽  
Vol 48 (9) ◽  
pp. 1066-1078 ◽  
Author(s):  
S. Pootrakul ◽  
G. H. Dixon
Keyword(s):  
Acetic Acid ◽  
Gel Electrophoresis ◽  
Cyanogen Bromide ◽  
Starch Gel Electrophoresis ◽  
Abnormal Hemoglobin ◽  
Starch Gel ◽  
Α Chain ◽  
Acid Alteration ◽  
Peptide Maps ◽  
Amino Acid Alteration

A slow (less anionic) hemoglobin mutant has been detected by starch gel electrophoresis of hemoglobin from three unrelated patients in Bangkok. Dissociation of the abnormal hemoglobin with p-hydroxymercuribenzoate showed that the α-chain was the site of the mutation. The mutant α-chain was isolated by carboxymethylcellulose chromatography in 8 M urea and 0.05 M β-mercaptoethanol. Peptide maps of trypsin and cyanogen bromide cleaved α-chain indicated that the amino acid alteration of the mutant was in the peptide corresponding to residues 62–76 of the α-chain. Further cleavage of this peptide with 0.25 M acetic acid at 110 °C showed that residue 74 was changed from an aspartyl to a histidyl residue, a mutation not previously described. It is proposed that this new hemoglobin α274His β2A be called hemoglobin Mahidol after Mahidol University in Bangkok. In one of the three patients showing hemoglobin Mahidol, interaction with α-thalassemia occurs and, in this patient, hemoglobin A is totally absent, being replaced by hemoglobin Mahidol together with some hemoglobin H (β4A).

scholarly journals The Fractionation of ?-Histones From Chicken Erythrocyte Nuclei

1964 ◽  
Vol 17 (4) ◽  
pp. 1001 ◽  
Author(s):  
JT Bellair ◽  
OM Mauritzen
Keyword(s):  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Gel Electrophoresis ◽  
Starch Gel Electrophoresis ◽  
Chicken Erythrocyte ◽  
Exclusion Chromatography ◽  
Starch Gel

Crude IX-histone, obtained from the original histone complex by precipitation of the f3-and y-histones with ethanol, has been shown by starch-gel electrophoresis to contain 13 components. The fractionation of IX-histone by exclusion chromatography on Sephadex G-200 is reported. While none of these components have been obtained pure in the present study, considerable purification of components 2, 3, 4, 5, 8, 9, 10, and 11 has been achieved, and their amino acid composition leaves no doubt that o::-histones represent a muoh larger family of "lysine-rich" proteins than was hitherto supposed.

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