scholarly journals The amino acid sequence of Helianthus annuus L (sunflower) cytochrome c deduced from chymotrypic peptides

1970 ◽  
Vol 119 (3) ◽  
pp. 535-539 ◽  
Author(s):  
J. A. M. Ramshaw ◽  
E. W. Thompson ◽  
D. Boulter
Keyword(s):  
Amino Acid ◽  
Cytochrome C ◽  
Amino Acid Sequence ◽  
Amino Acid Composition ◽  
Helianthus Annuus ◽  
Acid Composition ◽  
Mung Bean ◽  
Wheat Germ ◽  
Paper Electrophoresis ◽  
Complete Sequence

Peptides derived from digestion of 1 μmol of sunflower cytochrome c with chymotrypsin were separated by paper electrophoresis. The sequences of these peptides were determined by using the dansyl–Edman method (Gray & Hartley, 1963) and confirmed by analysis of their amino acid composition. Comparison of the set of peptides with the chymotryptic peptides of mung-bean (Thompson, Laycock, Ramshaw & Boulter, 1970) and wheat germ (Stevens, Glazer & Smith, 1967) cytochrome c shows a clear homology. The complete sequence of sunflower cytochrome c was established by alignment of the sunflower peptides with the sequences of mung bean cytochrome c and wheat germ cytochrome c.

scholarly journals A collagen-like amino acid sequence in a polypeptide chain of human C1q (a subcomponent of the first component of complement)

1974 ◽  
Vol 141 (1) ◽  
pp. 189-203 ◽  
Author(s):  
Kenneth B. M. Reid
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Polypeptide Chain ◽  
Complete Sequence ◽  
Partial Amino Acid Sequence ◽  
Collagenase Digestion ◽  
A Chain

1. A partial amino acid sequence of 95 residues of the 191 residues in the oxidized A chain of human subcomponent C1q was determined. The partial nature of the sequence is because one overlapping peptide is missing in the proposed sequence, also the proof of some of the overlapping peptides depends partly on their amino acid composition and not on their complete sequence. 2. This region of the A chain contained a repeating sequence of glycine-X-Y (where X is often proline and Y is often hydroxyproline) for 78 residues. 3. The five hydroxylysine residues and the five hydroxyproline residues present in the oxidized A chain were all in these 78 residues and only in the Y position of the repeating sequence. 4. Prolonged collagenase digestion of the oxidized A chain yielded a large, apparently C-terminal, peptide which contained most of the non-collagenous sequences present in the chain. 5. It is concluded that there is a collagen-like region in the A chain of subcomponent C1q which constitutes most of the N-terminal half of the chain and that similar collagen-like regions will be found in the B and C chains.

scholarly journals The amino acid sequence of Phaseolus aureus L. (mung-bean) cytochrome c

1970 ◽  
Vol 117 (1) ◽  
pp. 183-192 ◽  
Author(s):  
E. W. Thompson ◽  
M. V. Laycock ◽  
J. A. M. Ramshaw ◽  
D. Boulter
Keyword(s):  
Amino Acid ◽  
Cytochrome C ◽  
Amino Acid Sequence ◽  
Mung Bean ◽  
Wheat Germ ◽  
Amino Acid Residues ◽  
Phaseolus Aureus ◽  
Single Polypeptide Chain ◽  
Cytochromes C ◽  
Lysine Residues

The amino acid sequence of Phaseolus aureus L. (mung-bean) cytochrome c has been determined. The molecule consists of a single polypeptide chain of 111 amino acid residues and is homologous with other mitochondrial cytochromes c. Comparison with the amino acid sequence of wheat-germ cytochrome c (Stevens, Glazer & Smith, 1967) shows 14 differences. On alignment with mammalian cytochromes c, mung-bean cytochrome c has an N-acetylated ‘tail’ of eight amino acid residues similar to that found in wheat-germ cytochrome c. Of the 22 positions in wheat-germ cytochrome c that contain amino acid residues unique to these positions, 20 were found to contain the same ones in mung-bean cytochrome c. The ∈-N-trimethyl-lysine residues reported for wheat-germ cytochrome c (Delange, Glazer & Smith, 1969) in positions 72 and 86 were also found in these positions in mung-bean cytochrome c. The sequence was determined from 3μmol, by using chymotryptic and tryptic peptides which were analysed by the ‘dansyl’–Edman method (Gray & Hartley, 1963a), with confirmation by amino acid analysis.

scholarly journals The Amino Acid Sequence of Wheat Germ Cytochrome c

1967 ◽  
Vol 242 (11) ◽  
pp. 2764-2779
Author(s):  
Frits C. Stevens ◽  
A.N. Glazer ◽  
Emil L. Smith
Keyword(s):  
Amino Acid ◽  
Cytochrome C ◽  
Amino Acid Sequence ◽  
Wheat Germ

GENETIC VARIATION IN THE NEUROHYPOPHYSIAL HORMONES OF THE MOUSE, MUS MUSCULUS

1971 ◽  
Vol 51 (1) ◽  
pp. 191-201 ◽  
Author(s):  
A. D. STEWART
Keyword(s):  
Genetic Variation ◽  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Paper Electrophoresis ◽  
Neurohypophysial Hormones ◽  
Lysine Vasopressin ◽  
The Difference ◽  
Evolutionary Consequences ◽  
Layer Chromatography

SUMMARY The possibility of genetic variation in the amino acid composition of neurohypophysial hormones of the mouse was investigated. Acetic acid extracts from acetone-dried neurohypophyses from six strains of mice were subjected to thin-layer chromatography. Extracts from two strains were tested for natriferic potency on a toad bladder preparation. Extracts from three strains of mice were purified on a carboxymethylcellulose column, and the amino acid composition determined by paper electrophoresis at pH 2. All six strains of mice were found to elaborate an oxytocic principle with the chromatographic properties of oxytocin. All results were compatible with the view that five of the strains elaborate the usual mammalian vasopressin, [8-arginine]-vasopressin. However, chromatography, natriferic assays and analyses of amino acid composition indicated that the Peru strain of mice elaborated [8-lysine]-vasopressin. These mice would be the first mammals outside the Suina which possess this hormone, and the difference between the strains of mice is almost certainly genetic in origin. The significance of genetic variation within a species in the structure of a hormone is discussed in terms of its physiological and evolutionary consequences.

scholarly journals Determination of Amino Acid Composition of Ganirelix Acetate in an Injectable Formulation by Pre-column Derivatization with 6-Aminoquinolyl-N-hydroxysuccinimidyl Carbamate

2020 ◽  
Vol 58 (8) ◽  
pp. 687-694
Author(s):  
Kumarswamy Ummiti ◽  
J V Shanmukha Kumar
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Flash Chromatography ◽  
Molar Ratio ◽  
Acid Mixture ◽  
Injectable Formulation

Abstract Ganirelix is a synthetic decapeptide linked with nine different amino acids. To understand the peptide amino acid sequence or primary structure, the first step is to determine the amino acid composition of the peptide which can be a determining factor for the peptide immunogenicity. Edman degradation is not a suitable analytical technique to identify amino acid sequence present in Ganirelix due to the absence of uncharged N-terminal amino group. To address this challenge, a pre-column derivatization method was developed with 6-aminoquinolyl-N-hydroxysuccinimidyl carbamate reagent. In the present work, the Ganirelix active pharmaceutical ingredient present in the injectable formulation was isolated by fraction collection and further purified by flash chromatography. The amino acid composition of Ganirelix is assayed by carrying out acid hydrolysis with 6 mol L−1 hydrochloric acid solution containing 1% phenol at 100°C for 24 h and derivatization with 6-aminoquinolyl-N-hydroxysuccinimidyl carbamate reagent solution, followed by determination of individual amino acids by reverse-phase chromatography using a C18 column. High resolution was achieved for the nine amino acid mixture. The amino acid composition results of temperature-stressed Ganirelix generic product and reference listed drug are in good agreement with the theoretical molar ratio of label information.

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