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 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.

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.

scholarly journals Localization and Characterization of the Cleavage-Associated Neoantigen in the Edomain of Fibrinogen

1977 ◽  
Author(s):  
E. F. Plow ◽  
T. S. Edgington
Keyword(s):  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Conformational Changes ◽  
Deae Cellulose ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Amino Terminal ◽  
Exclusion Chromatography

Plasmic cleavage of fibrinogen to generate fragment X partially exposes a specific cryptic molecular site, fg-Eneo. This site in the E domain of the molecule is further exposed during subsequent cleavage. We now report on localization of this site which provides an incisive marker for the structural and conformational changes associated with plasmic cleavage of fibrinogen. Fg-Eneo was stable to reduction and alkylation and the chains of the E fragment were separated by ion exchange chromatography on DEAE-cellulose. An active component was obtained and subjected to molecular exclusion chromatography on Sephadex G-50 to insure removal of intact fg-E. A fg-Eneo positive chain was recovered and identified as Eγ with respect to amino-terminal tyrosine, amino acid composition, and immunochemical analysis. The fg-Eneo site was stable to tryptic degradation, and tryptic peptides were prepared and separated by multiple molecular exclusion chromatographic steps. Final separation of two peptides of similar size was achieved on the basis of carbohydrate content by affinity chromatography on Concanavalin A. Only the active peptide was bound by the lectin. Purity and identification of the active tryptic peptide as γ36–53 was established by amino acid composition and sequence. These results establish that this region of the γ chain of fibrinogen is not present at the hydrated surface of the native molecule but that, in association with plasmic cleavage and conformational changes, this site is progressively exposed and provides a dynamic marker of the cleavage sequence.

scholarly journals Characterization of Human KAP24.1, A Cuticular Hair Keratin-Associated Protein with Unusual Amino-Acid Composition and Repeat Structure

2007 ◽  
Vol 127 (5) ◽  
pp. 1197-1204 ◽  
Author(s):  
Michael A. Rogers ◽  
Hermelita Winter ◽  
Lutz Langbein ◽  
Anke Wollschläger ◽  
Silke Praetzel-Wunder ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Repeat Structure ◽  
Hair Keratin ◽  
Unusual Amino Acid
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