Complete amino acid sequence of a papain-solubilized human histocompatibility antigen, HLA-B7. 1. Isolation and amino acid composition of fragments and of tryptic and chymotryptic peptides

Biochemistry ◽  
1979 ◽  
Vol 18 (25) ◽  
pp. 5704-5711 ◽  
Author(s):  
Jose A. Lopez de Castro ◽  
Harry T. Orr ◽  
Richard J. Robb ◽  
Thomas G. Kostyk ◽  
Dean L. Mann ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Histocompatibility Antigen ◽  
Complete Amino Acid Sequence

scholarly journals Complete Amino Acid Sequence of the N-Terminal Cyanogen Bromide Fragment CNBr-3 From a Microfibrillar Protein From Wool

1980 ◽  
Vol 33 (3) ◽  
pp. 295 ◽  
Author(s):  
Keith H Gough ◽  
Adam S Inglis
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Cyanogen Bromide ◽  
Edman Degradation ◽  
Complete Amino Acid Sequence ◽  
Sequence Homologies ◽  
Low Sulfur ◽  
Cyanogen Bromide Fragment

The amino acid sequence of a 59-residue 'non-helical tail' from a low-sulfur microfibrillar protein (component 8c-I) from wool is reported. The amino acid composition shows relatively high contents of serine (17 %), half-cystine (14 %), proline (8 %), glycine (8 %) compared to the helical areas of component 8c-I. Although the composition of the cyanogen bromide fragment CNBr-3 resembles the compositions of the high-sulfur proteins extracted from wool there are no obvious sequence homologies present. The Edman degradation yields at an aspartyl-glycyl bond decreased so much that difficulties were encountered in determining the subsequent sequence.

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.

scholarly journals Glyceraldehyde-3 Phosphate Dehydrogenase From the Red Kangaroo (Megalelia Rufa): Purification and the Amino Acid Sequence Around a Reactive Cysteine

1971 ◽  
Vol 24 (2) ◽  
pp. 263 ◽  
Author(s):  
RJ Simpson ◽  
BE Davidson
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Amino Acid Sequences ◽  
Red Kangaroo ◽  
Leg Muscle

Glyceraldehyde-3-phosphate dehydrogenase from leg muscle of M. rufa has been extracted and purified. The reaction of the enzyme with iodoacetate, the amino acid composition, tryptic fingerprint, and some amino acid sequences (in-cluding that around the reactive cysteine) indicate that kangaroo glyceraldehyde-3-phosphate dehydrogenase is almost identical with pig glyceraldehyde-3-phosphate dehydrogenase.

Amino Acid Composition and NH2-Terminal Amino Acid Sequence of Rat Platelet Secretory Phospholipase A21

1987 ◽  
Vol 101 (5) ◽  
pp. 1311-1314 ◽  
Author(s):  
Makio HAYAKAWA ◽  
Kazuhiko HORIGOME ◽  
Ichiro KUDO ◽  
Motowo TOMITA ◽  
Shoshichi NOJIMA ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Terminal Amino Acid ◽  
Secretory Phospholipase ◽  
Terminal Amino ◽  
Terminal Amino Acid Sequence

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.

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