Characterization of protein, peptide and amino acid fouling on ion-exchange and filtration membranes: Review of current and recently developed methods

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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Triple-column ion-exchange physiological amino acid analysis with fluorescent detection: Baseline characterization of human cerebrospinal fluid

Analytical Biochemistry ◽

10.1016/0003-2697(84)90561-x ◽

1984 ◽

Vol 143 (1) ◽

pp. 82-94 ◽

Cited By ~ 35

Author(s):

Thomas N. Ferraro ◽

Theodore A. Hare

Keyword(s):

Cerebrospinal Fluid ◽

Amino Acid ◽

Ion Exchange ◽

Amino Acid Analysis ◽

Fluorescent Detection ◽

Human Cerebrospinal Fluid

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PURIFICATION AND PARTIAL CHEMICAL CHARACTERIZATION OF SHEEP NEUROPHYSIN

Acta Endocrinologica ◽

10.1530/acta.0.0740226 ◽

1973 ◽

Vol 74 (2) ◽

pp. 226-236 ◽

Cited By ~ 6

Author(s):

Michel Chrétien ◽

Claude Gilardeau

Keyword(s):

Amino Acid ◽

Polyacrylamide Gel Electrophoresis ◽

Chemical Characterization ◽

Terminal Amino Acid ◽

Amino Acid Determination ◽

Pituitary Glands ◽

Terminal Amino ◽

Partial Chemical ◽

Acid Determination

ABSTRACT A protein isolated from ovine pituitary glands has been purified, and its homogeneity assessed by NH2- and COOH-terminal amino acid determination, ultracentrifugation studies, and polyacrylamide gel electrophoresis after carboxymethylation. Its chemical and immunochemical properties are closely similar to those of beef and pork neurophysins, less similar to those of human neurophysins. It contains no tryptophan (like other neurophysins) or histidine (like all except bovine neurophysin-I and human neurophysins). It has alanine at the NH2-terminus and valine at the COOH-terminus. Its amino acid composition is similar to, but not identical with those of porcine and bovine neurophysins.

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