scholarly journals Improved purification and characterization of the OXA-2 β-lactamase

1984 ◽  
Vol 224 (3) ◽  
pp. 1009-1013 ◽  
Author(s):  
S Holland ◽  
J W Dale
Keyword(s):  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Terminal Region ◽  
Beta Lactamase ◽  
Purification And Characterization

An improved and scaled-up procedure has been developed for purifying the OXA-2 plasmid-mediated beta-lactamase. This has enabled us to improve the characterization of this enzyme, including a revised determination of its amino acid composition and the sequence of the N-terminal region of the protein.

Purification and characterization of porcine κ-casein

1984 ◽  
Vol 51 (2) ◽  
pp. 259-266 ◽  
Author(s):  
Jutta Cerning-Beroard ◽  
Claude Zevaco
Keyword(s):  
Amino Acid ◽  
Affinity Chromatography ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Sugar Composition ◽  
Purification And Characterization ◽  
Acetylneuraminic Acid ◽  
Porcine Milk

Summaryκ-casein from porcine milk was isolated and purified by affinity chromatography on thiopropyl Sepharose followed by hydroxyapatite chromatography. The amino acid composition of this protein is similar to that of bovine κ-casein. The sugar composition was established and sow κ-casein was found to be highly glycosylated. It contains 12 N-acetylneuraminic acid, 10 N-acetylgalactosamine, 2 N-acetylglucosamine and 22 galactose residues.

scholarly journals Separation and partial characterization of guinea-pig caseins

1978 ◽  
Vol 173 (2) ◽  
pp. 633-641 ◽  
Author(s):  
R K Craig ◽  
D McIlreavy ◽  
R L Hall
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Guinea Pig ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Gel Filtration ◽  
Exchange Chromatography

1. Guinea-pig caseins A, B and C were purified free of each other by a combination of ion-exchange chromatography and gel filtration. 2. Determination of the amino acid composition showed all three caseins to contain a high proportion of proline and glutamic acid, but no cysteine. This apart, the amino acid composition of the three caseins was markedly different, though calculated divergence values suggest that some homology may exist between caseins A and B. Molecular-weight estimates based on amino acid composition were in good agreement with those based on sodium dodecyl sulphate/polyacrylamide-gel electrophoresis. 3. N-Terminal analysis showed lysine, methionine and lysine to be the N-terminal residues of caseins A, B and C respectively. 4. Two-dimensional separation of tryptic digests revealed a distinctive pattern for each casein. 5. All caseins were shown to be phosphoproteins. The casein C preparation also contained significant amounts of sialic acid, neutral and amino sugars. 6. The results suggest that each casein represents a separate gene product, and that the low-molecular-weight proteins are not the result of a post-translational cleavage of the largest. All were distinctly different from the whey protein alpha-lactalbumin.

scholarly journals Studies on the Determination of Amino Acid Composition of Food Proteins (Part 2)

1964 ◽  
Vol 17 (4) ◽  
pp. 283-285
Author(s):  
Takao Shinagawa ◽  
Toshio Habu ◽  
Akemi Murakami
Keyword(s):  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Food Proteins

scholarly journals Determination of Amino Acid Composition in the Harpagophytum procumbens Root

2019 ◽  
Vol 18 (1) ◽  
pp. 85-91
Author(s):  
AI Kriukova ◽  
IM Vladymyrova ◽  
OL Levashova ◽  
TS Tishakova
Keyword(s):  
Amino Acids ◽  
High Performance Liquid Chromatography ◽  
Liquid Chromatography ◽  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
High Performance ◽  
Harpagophytum Procumbens

The amino acid composition of the roots of Harpagophytum procumbens was investigated by the method of high performance liquid chromatography (HPLC) with preliminary derivatization. Sixteen free and thirteen bound amino acids were quantitatively determined. The content of protein-bound amino acids was calculated. Dhaka Univ. J. Pharm. Sci. 18(1): 85-91, 2019 (June)

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 High-Sulphur Proteins From a-Keratins ll. Isolation and Partial Characterization of Purified Components From Mouse Hair

1976 ◽  
Vol 29 (2) ◽  
pp. 11 ◽  
Author(s):  
Robert C Marshall ◽  
JM Gillespie
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Ion Exchange ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Fractional Precipitation ◽  
Molecular Weight Range

The present paper continues the study of the reduced and S-carboxymethylated high-sulphur proteins from mouse hair. Fractions have been obtained in a substantially purified form by fractional precipitation with ammonium sulphate at pH 6, followed by ion exchange chromatography on cellulose phosphate at pH 2�6. Approximately 80% by weight of the high-sulphur proteins fall into the ultra-high-sulphur category (carboxymethyicysteine content greater than 26 residues per 100 residues), and they cover a molecular weight range of 17000-28000. The components show a remarkable diversity in amino acid composition; for example the contents of arginine and glycine each vary by about 3 : 1. The remainder of the proteins contain 17-20 residues per 100 residues of carboxymethyicysteine, are smaller in size (molecular weight 11 500), and also show great diversity in overall amino acid composition.

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