scholarly journals Comparative studies of two types of bovine immunoglobulin G heavy chains

1968 ◽  
Vol 107 (4) ◽  
pp. 559-564 ◽  
Author(s):  
C. P. Milstein ◽  
A. Feinstein
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Immunoglobulin G ◽  
Comparative Studies ◽  
Cyanogen Bromide ◽  
Serum Immunoglobulin ◽  
Heavy Chains ◽  
Bovine Immunoglobulin

‘Fingerprints’ of bovine colostrum and serum immunoglobulin G1 heavy chains were extremely similar, but different from serum immunoglobin G2 heavy chains. Serum immunoglobulin G1 and immunoglobulin G2 heavy chains were treated with cyanogen bromide. The fractions from the C-terminal end of the heavy chains were isolated and the amino acid sequence of this fraction from immunoglobulin G2 was:His-Glx-Ala-Leu-His-Asx-His-Tyr-Met-Gln-Lys-Ser-Thr-Ser-Lys-Ser-Ala-GlyThe amino acid composition of this fraction from immunoglobulin G1 was the same except for the methionine, which in immunoglobulin G1 was replaced by threonine.

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 Molecular Cloning of the Pasteurella haemolytica pomA Gene and Identification of Bovine Antibodies against PomA Surface Domains

1999 ◽  
Vol 67 (9) ◽  
pp. 4968-4973 ◽  
Author(s):  
Hui Zeng ◽  
Karamjeet Pandher ◽  
George L. Murphy
Keyword(s):  
Amino Acid ◽  
Nucleotide Sequence ◽  
Membrane Protein ◽  
Amino Acid Sequence ◽  
Outer Membrane Protein ◽  
Immunoglobulin G ◽  
Pasteurella Haemolytica ◽  
Respiratory Pathogen ◽  
Surface Domains ◽  
Bovine Immunoglobulin

ABSTRACT The gene (pomA) encoding PomA, an OmpA-like major outer membrane protein of the bovine respiratory pathogen Pasteurella haemolytica, was cloned, and its nucleotide sequence was determined. The deduced amino acid sequence of PomA has significant identity with the sequences of other OmpA family proteins. Absorption of three different bovine immune sera with whole P. haemolytica cells resulted in a reduction of bovine immunoglobulin G reactivity with recombinant PomA in Western immunoblots, suggesting the presence of antibodies against PomA surface domains.

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.

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