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 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 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.

scholarly journals The Amino Acid Composition of Hemoglobin. V. The Preparation of Purified Hemoglobin Fractions by Chromatography on Cellulose Exchangers and Their Identification by Starch Gel Electrophoresis Using Tris-Borate-EDTA Buffer

Blood ◽  
1965 ◽  
Vol 25 (5) ◽  
pp. 646-661 ◽  
Author(s):  
AMOZ I. CHERNOFF ◽  
NELSON PETTIT ◽  
JO NORTHROP
Keyword(s):  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Chromatographic Separation ◽  
Gel Electrophoresis ◽  
Starch Gel Electrophoresis ◽  
Starch Gel ◽  
Tris Borate Edta

Abstract The chromatographic separation of hemoglobin on two cellulose exchangers, CMC and DEAE, is discussed. Problems related to the use of these technics are described. In addition, our experience with the use of Tris-Borate-EDTA buffer (Smithies) for hemoglobin electrophoresis in starch gel is presented.

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.

scholarly journals Studies on Reduced Wool III. Starch-Gel Electrophoresis of Extracted Wool Proteins

1964 ◽  
Vol 17 (1) ◽  
pp. 277 ◽  
Author(s):  
EOP Thompson ◽  
IJ O'donnell
Keyword(s):  
Gel Electrophoresis ◽  
Moving Boundary ◽  
Electrophoretic Pattern ◽  
Deae Cellulose ◽  
Protein Fractions ◽  
Single Peak ◽  
Starch Gel Electrophoresis ◽  
Starch Gel ◽  
Wool Proteins

Starch-gel electrophoresis in 8M urea has been used to demonstrate the presence of many components in wool protein fractions extracted from reduced and alkylated wool. All preparations of low-sulphur wool proteins gave mUltiple bands on starch gel in 8M urea even though some of these had previously been fractionated to give a single peak using moving-boundary electrophoresis in the absence of 8M urea. The heterogeneity suggested by these results is in Rccord with that found by chromatography of the proteins on DEAE-cellulose in buffers containing 8M urea. With stepwise elution from DEAE-cellulose it is possible to obtain fractions responsible for various sections of the starch-gel electrophoretic pattern.

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 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 MICROTUBULE PROTEIN

1971 ◽  
Vol 51 (1) ◽  
pp. 138-147 ◽  
Author(s):  
Howard Feit ◽  
Gary R. Dutton ◽  
Samuel H. Barondes ◽  
Michael L. Shelanski
Keyword(s):  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Gel Electrophoresis ◽  
Soluble Protein ◽  
Peptide Mapping ◽  
Nerve Endings ◽  
Subunit Protein ◽  
Microtubule Protein ◽  
Slow Transport

The subunit protein of microtubules, tubulin, has been demonstrated to be present in isolated nerve endings by gel electrophoresis, amino acid composition, and peptide mapping. The tubulin constitutes approximately 28% of the soluble protein of the nerve endings. The transport of tubulin to the nerve endings has been demonstrated and its relationship to slow transport is discussed.

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.

scholarly journals Purification and biochemical characterization of three major acidic proteins (BSP-A1, BSP-A2 and BSP-A3) from bovine seminal plasma

1987 ◽  
Vol 241 (3) ◽  
pp. 685-692 ◽  
Author(s):  
P Manjunath ◽  
M R Sairam
Keyword(s):  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Seminal Plasma ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Gel Filtration ◽  
Polyacrylamide Gel ◽  
Terminal Residue ◽  
Acidic Proteins

Three major acidic proteins of bovine seminal plasma, BSP-A1, BSP-A2 and BSP-A3, were purified to homogeneity, by employing fast protein liquid chromatography, gel filtration and h.p.l.c. The proteins were purified on the basis of their stimulatory effect on the basal release of gonadotropins by rat anterior-pituitary cells in culture. All three proteins migrated as distinct single bands in the presence or absence of 2-mercaptoethanol in SDS/polyacrylamide-gel electrophoresis. Their Mr values were estimated to be between 15,000 and 16,500 by SDS/polyacrylamide-gel electrophoresis. Similar Mr estimates were obtained when they were subjected to gel filtration on a calibrated column of Sephadex G-75 equilibrated in 0.05 M-acetic acid, pH 3.0. However, BSP-A1 and BSP-A2 were eluted as aggregated molecules (Mr 60,000-120,000) during gel filtration on Sephadex G-200 equilibrated in 0.05 M-NH4HCO3, pH 8.5, or phosphate buffer, pH 7.0, containing 0.15 M-NaCl. In the presence of 8 M-urea both BSP-A1 and BSP-A2 were eluted at positions corresponding to Mr values of 17,000-20,000. BSP-A1 and BSP-A2 had an identical amino acid composition, which differed largely from that of BSP-A3. All three proteins contained aspartic acid as the N-terminal residue, and cysteine was identified as the C-terminal residue. BSP-A1 and BSP-A2 are glycoproteins containing galactosamine, sialic acid and neutral sugars, but BSP-A3 did not contain any covalently attached sugars. Whereas BSP-A2 and BSP-A3 were eluted unadsorbed, BSP-A1 bound to wheat-germ lectin-Sepharose 6MB and could be eluted by the competing sugar N-acetyl-D-glucosamine. Treatment of BSP-A1 and BSP-A2 with trypsin resulted in complete loss of gonadotropin-release activity, but BSP-A3 retained full activity. Antibody raised against BSP-A1 did not cross-react with BSP-A3, or vice versa. All these properties indicated marked structural differences between BSP-A3 and BSP-A1 (or BSP-A2). On the basis of amino acid composition it was concluded that BSP-A1, BSP-A2 and BSP-A3 are the same as the gonadostatins [Esch, Ling, Bohlen, Ying & Guillemin (1983) Biochem. Biophys. Res. Commun. 113, 861-867].

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