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 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 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 Ribitol dehydrogenase from Klebsiella aerogenes. Purification and subunit structure

1974 ◽  
Vol 141 (3) ◽  
pp. 693-700 ◽  
Author(s):  
Susan S. Taylor ◽  
Peter W. J. Rigby ◽  
Brian S. Hartley
Keyword(s):  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Subunit Structure ◽  
Klebsiella Aerogenes ◽  
Peptide Maps ◽  
Ribitol Dehydrogenase

Ribitol dehydrogenase has been purified to homogeneity from several strains of Klebsiella aerogenes. One strain yields 3–6g of pure enzyme from 1kg of cells. The enzyme is a tetramer of four subunits, mol.wt. 27000. Preliminary studies of the activity of the enzyme are reported. Peptide ‘maps’ together with the amino acid composition indicate that the subunits are identical.

scholarly journals Cationic Proteins of Human Granulocytes. II. Separation of the Cationic Proteins of the Granules of Leukemic Myeloid Cells

Blood ◽  
1974 ◽  
Vol 44 (2) ◽  
pp. 235-246 ◽  
Author(s):  
I. Olsson ◽  
P. Venge
Keyword(s):  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Aminocaproic Acid ◽  
Cationic Protein ◽  
Cationic Proteins ◽  
Molecular Weights ◽  
Electrophoretic Mobilities ◽  
Human Granulocytes ◽  
Protein Components

Abstract The highly cationic proteins of human granulocytes, whose electrophoretic mobilities toward the cathode are faster than that for lysozyme, were isolated from the cytoplasmic granules of leukocytes, obtained from patients with chronic myeloid leukemia. The granule extract was subjected to chromatography on Sephadex G-75 and E-aminocaproic acid-Sepharose ion adsorbant followed by preparative electrophoresis on agarose. Seven cationic protein components were identified, and five of these were obtained in a pure form. One group of cationic proteins, including components 1-4, exhibited molecular weights in the range 25,500-28,500, almost identical amino acid composition, and complete immunologic identity. Another group of proteins, including components 5-7, exhibited molecular weights in the range 21,000-29,000 and also showed complete immunologic identity; amino acid analysis performed on component 5 indicated a different amino acid composition from that of components 1-4. Cationic proteins with similar electrophoretic mobilities and immunochemical identities were also detected in granule extracts of granulocytes from healthy individuals. The proteins isolated from human granulocytes have a higher molecular weight and a lower content of basic amino acids than the cationic proteins with antibacterial and permeability-increasing properties previously demonstrated in rabbit polymorphonuclear granulocytes.

Proteins in the Enamel Fluid of Immature Porcine Teeth

1987 ◽  
Vol 66 (12) ◽  
pp. 1721-1726 ◽  
Author(s):  
T. Aoba ◽  
T. Tanabe ◽  
E.C. Moreno
Keyword(s):  
Amino Acid ◽  
Amino Acid Composition ◽  
Protein Content ◽  
Acid Composition ◽  
Permanent Teeth ◽  
Major Protein ◽  
Protein Species ◽  
Terminal Sequence ◽  
Molecular Weights ◽  
Sds Electrophoresis

The fluid was separated from the immature soft enamel of porcine permanent teeth in the secretory stage according to procedures reported previously (Aoba and Moreno, 1987). The protein content of the fluid was about 2.8% w/v; its amino-acid composition was characterized by high contents of Pro, Glx, Leu, and His, showing composition similar to that of the 20 kilo-dalton (kd) amelogenin or its C-terminal segments. The two major protein species in the fluid had apparent molecular weights of 13 kd and 11 kd, as determined by SDS electrophoresis; the N-terminal residue of the former was Leu, while that of the latter was Ala. The C-terminal sequence of both of them was -Met-Phe-Ser. By comparison with the published sequence of 20-kd porcine amelogenin, it is concluded that the main fluid constituents were derived by cleavages of N-terminal segments from the 20-kd amelogenin.

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 Localization and Characterization of the Cleavage-Associated Neoantigen in the Edomain of Fibrinogen

1977 ◽  
Author(s):  
E. F. Plow ◽  
T. S. Edgington
Keyword(s):  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Conformational Changes ◽  
Deae Cellulose ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Amino Terminal ◽  
Exclusion Chromatography

Plasmic cleavage of fibrinogen to generate fragment X partially exposes a specific cryptic molecular site, fg-Eneo. This site in the E domain of the molecule is further exposed during subsequent cleavage. We now report on localization of this site which provides an incisive marker for the structural and conformational changes associated with plasmic cleavage of fibrinogen. Fg-Eneo was stable to reduction and alkylation and the chains of the E fragment were separated by ion exchange chromatography on DEAE-cellulose. An active component was obtained and subjected to molecular exclusion chromatography on Sephadex G-50 to insure removal of intact fg-E. A fg-Eneo positive chain was recovered and identified as Eγ with respect to amino-terminal tyrosine, amino acid composition, and immunochemical analysis. The fg-Eneo site was stable to tryptic degradation, and tryptic peptides were prepared and separated by multiple molecular exclusion chromatographic steps. Final separation of two peptides of similar size was achieved on the basis of carbohydrate content by affinity chromatography on Concanavalin A. Only the active peptide was bound by the lectin. Purity and identification of the active tryptic peptide as γ36–53 was established by amino acid composition and sequence. These results establish that this region of the γ chain of fibrinogen is not present at the hydrated surface of the native molecule but that, in association with plasmic cleavage and conformational changes, this site is progressively exposed and provides a dynamic marker of the cleavage sequence.

scholarly journals The Macroheterogeneity of Type I Tyrosine-rich Proteins of Merino Wool

1974 ◽  
Vol 27 (6) ◽  
pp. 617 ◽  
Author(s):  
J M Gillespie ◽  
MJ Frenkel
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Quaternary Ammonium ◽  
Deae Cellulose ◽  
Type I ◽  
Merino Wool ◽  
Poor Family ◽  
Tyrosine Content

The cystine-poor family of tyrosine-rich proteins of wool as their S-carboxymethyl derivatives has been shown by chromatography on quaternary ammonium ethylcellulose (QAE-cellulose) at pH 10� 5 to consist of 10 groups of proteins which span a threefold range of tyrosine content and vary in many other amino acids, particularly S-carboxymethylcysteine. Electrophoresis at pH 8�9 revealed that most fractions contain two or more components and by further chromatography of five of these groups at pH 8�3 on DEAE-cellulose 10 components have been isolated. The amino acid composition suggests that the components within each QAE-cellulose group are very closely related.

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