scholarly journals Amino acid sequences of peptides from a chymotryptic digest of a urea-soluble protein fraction (U.S.3) from oxidized wool

1969 ◽  
Vol 115 (2) ◽  
pp. 323-334 ◽  
Author(s):  
M. C. Corfield ◽  
J. C. Fletcher
Keyword(s):  
Amino Acid ◽  
Cation Exchange ◽  
Protein Fraction ◽  
Exchange Resin ◽  
Cation Exchange Resin ◽  
Paper Electrophoresis ◽  
Amino Acid Sequences ◽  
Amino Acid Residues ◽  
Soluble Protein Fraction ◽  
Peptide Fractions

1. A chymotryptic digest of the protein fraction U.S.3. from oxidized wool was separated into 51 peptide fractions by chromatography on a column of cation-exchange resin. 2. The less acidic fractions were separated into their component peptides by a combination of cation-exchange-resin chromatography, paper chromatography and paper electrophoresis. 3. The amino acid sequences of 34 of these peptides were elucidated, and those of 14 others partially determined. 4. Overlaps between the tryptic and chymotryptic peptides from fraction U.S.3 have enabled ten extended amino acid sequences to be deduced, the longest containing 20 amino acid residues. 5. The relevance of the results to the structures of the helical and non-helical regions of wool is discussed.

scholarly journals Amino acid sequences of peptides from a tryptic digest of a urea-soluble protein fraction (U.S.3) from oxidized wool

1967 ◽  
Vol 102 (3) ◽  
pp. 801-814 ◽  
Author(s):  
M. C. Corfield ◽  
J. C. Fletcher ◽  
A. Robson
Keyword(s):  
Amino Acid ◽  
Cation Exchange ◽  
Protein Fraction ◽  
Exchange Resin ◽  
Cation Exchange Resin ◽  
Paper Electrophoresis ◽  
Amino Acid Sequences ◽  
Tryptic Digest ◽  
Parent Protein ◽  
Wool Proteins

1. A tryptic digest of the protein fraction U.S.3 from oxidized wool has been separated into 32 peptide fractions by cation-exchange resin chromatography. 2. Most of these fractions have been resolved into their component peptides by a combination of the techniques of cation-exchange resin chromatography, paper chromatography and paper electrophoresis. 3. The amino acid compositions of 58 of the peptides in the digest present in the largest amounts have been determined. 4. The amino acid sequences of 38 of these have been completely elucidated and those of six others partially derived. 5. These findings indicate that the parent protein in wool from which the protein fraction U.S.3 is derived has a minimum molecular weight of 74000. 6. The structures of wool proteins are discussed in the light of the peptide sequences determined, and, in particular, of those sequences in fraction U.S.3 that could not be elucidated.

Isolation of Two Bovine Amelogenin Peptides and Their Amino Acid Sequences

1987 ◽  
Vol 1 (2) ◽  
pp. 276-281 ◽  
Author(s):  
J.-H. Yeh ◽  
T. Takagi ◽  
S. Sasaki
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Amino Acid Sequences ◽  
Polyacrylamide Gel ◽  
The Other ◽  
Edman Degradation ◽  
Amino Acid Residues ◽  
Peptide Fractions

Two peptide fractions of bovine amelogenin having a highly aggregative property to form polymers were purified by chromatography, SDS-polyacrylamide gel electrophoresis, and HPLC. Amino acid sequences of purified peptides were determined by automated Edman degradation. One peptide was found to be composed of 63 amino acid residues having a molecular weight of 7105, and the other of 86 residues having that of 9683. The sequence of the smaller peptide was identical to the C-terminal 63 residues of the amelogenin molecule of 170 residues previously reported, but the larger contained eight residues which are absent in the amelogenin sequence. There is a possibility that the latter peptide might be synthesized independently from mRNA spliced at different positions.

Divalent Amino Acid Adsorption on Cation Exchange Resin

2009 ◽  
Vol 44 (13) ◽  
pp. 3075-3087 ◽  
Author(s):  
Hidetada Nagai ◽  
Kazuhiro Hasegawa
Keyword(s):  
Amino Acid ◽  
Cation Exchange ◽  
Exchange Resin ◽  
Cation Exchange Resin

scholarly journals Isolation of bacilysin and a new amino acid from culture filtrates of Bacillus subtilis

1970 ◽  
Vol 118 (4) ◽  
pp. 557-561 ◽  
Author(s):  
J. E. Walker ◽  
E. P. Abraham
Keyword(s):  
Amino Acids ◽  
Bacillus Subtilis ◽  
Amino Acid ◽  
Glutamic Acid ◽  
Cation Exchange ◽  
Exchange Resin ◽  
Cation Exchange Resin ◽  
Neutral Amino Acids ◽  
Peptide Fraction ◽  
Neutral Peptide

1. Bacilysin, a labile dipeptide antibiotic that lyses growing staphylococci, was isolated from culture fluids of Bacillus subtilis by a process giving higher yields than those previously obtained. 2. The process involves adsorption on a cation-exchange resin and elution with aqueous trimethylamine, separation from neutral amino acids and glutamic acid by chromatography on DEAE-Sephadex at pH8.7 and separation from other neutral peptides by chromatography in aqueous propan-2-ol on Sephadex G-25. 3. A new amino acid, which is chemically related to bacilysin, was isolated from the fraction containing neutral amino acids. 4. Two substances that yield alanine on hydrolysis, in addition to bacilysin, were obtained from the neutral peptide fraction.

scholarly journals Neurotoxins from the venoms of the sea snakes Hydrophis ornatus and Hydrophis lapemoides

1983 ◽  
Vol 213 (1) ◽  
pp. 31-38 ◽  
Author(s):  
N Tamiya ◽  
N Maeda ◽  
H G Cogger
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Paper Electrophoresis ◽  
Amino Acid Sequences ◽  
British Library ◽  
Amino Acid Residues ◽  
Protein Amino Acid ◽  
Tryptic Peptides ◽  
Sea Snakes ◽  
And Migration

The main neurotoxic components, toxins Hydrophis ornatus a and Hydrophis lapemoides a, were isolated from the venoms of the sea snakes Hydrophis ornatus and Hydrophis lapemoides respectively. The amino acid sequence of toxin Hydrophis ornatus a was deduced to be identical with that of toxin Astrotia stokesii a [Maeda & Tamiya (1978) Biochem. J. 175, 507-517] on the basis of identity of the tryptic peptide ‘map’ and the amino acid composition of each peptide. The amino acid sequence of toxin Hydrophis lapemoides a was determined mainly on the basis of identity of the amino acid compositions, mobilities on paper electrophoresis and migration positions on paper chromatography of the tryptic peptides with those of other sea-snake toxins whose sequences are known. Both toxins Hydrophis ornatus a and Hydrophis lapemoides a consisted of 60 amino acid residues and there were six amino acid replacements between them. The taxonomy of sea snakes in the Hydrophis ornatus complex has long been confused, and the above snakes were originally assigned to taxa that proved to be inconsistent with the relationships indicated by the neurotoxin amino acid sequences obtained. A subsequent re-examination of the specimens revealed an error in the original identifications and demonstrated the value of the protein amino acid sequences in systematic and phylogenetic studies. The isolation procedure and results of amino acid analysis of the tryptic peptides have been deposited as Supplementary Publication SUP 50121 (8 pages) with the British Library Lending Division, Boston Spa, Wetherby, West Yorkshire LS23 7BQ, U.K., from whom copies may be obtained as indicated in Biochem. J. (1983) 209, 5.

The Amino Acid Sequence of Streptomyces griseus Protease A: The Peptic Peptides

1971 ◽  
Vol 49 (10) ◽  
pp. 1083-1097 ◽  
Author(s):  
P. Johnson ◽  
L. B. Smillie
Keyword(s):  
Amino Acid ◽  
Streptomyces Griseus ◽  
Disulfide Bridge ◽  
Exchange Chromatography ◽  
Amino Acid Sequences ◽  
Amino Acid Residues ◽  
Homologous Proteins ◽  
Acidic Peptide ◽  
Dowex 1 ◽  
Peptide Fractions

The peptic peptides of Streptomyces griseus Protease A (excluding the previously characterized disulfide bridge peptic peptides) were fractionated into basic, neutral, and neutral plus acidic peptide fractions by chromatography on Dowex 1 × 2. These three peptide fractions were then fractionated by cation-exchange chromatography on Chromobead P resin using the Technicon autoanalyzer system. Following further purifications on paper, the amino acid compositions and sequences of the peptic peptides were determined. The N-terminal sequence of Protease A has been identified as Ile–Ala–Gly–Gly–Glu–Ala. The numbers of amino acid residues obtained from the amino acid sequences reported are in agreement with those numbers obtained from amino acid analysis of the total protein in the cases of tryptophan, methionine, histidine, proline, phenylalanine, and glutamic acid. Some of the results suggest either the presence of nonidentical but highly homologous proteins in the Protease A preparation or the possibility of repeating sequences in a single molecular species.

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