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Adaptation of reverse-phase high-performance liquid chromatography for the isolation and sequence analysis of peptides from plasma amyloid P-component by Jacqueline K. Anderson; John E. Mole is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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Gel permeation and reverse-phase high-performance liquid chromatography were used to isolate chemical and enzymatic cleavage fragments of plasma amyloid P-component for amino acid sequence analysis. Optimal conditions for resolution of peptide mixtures were predetermined using analytical amounts (0.04-o. 1 nmol) and volatile trifluoroacetic acid-acetonitrile or ammonium acetate-acetonitrile buffer systems. Thereafter, 100-200 nmol of each hydrolyzate was chromatographed on preparative columns. Size-exclusion chromatography using an acetic acid solvent containing n-propanol was found to be most useful for large-molecularweight cyanogen bromide peptides while reverse-phase chromatography was best suited for the smaller enzymatically derived peptides. The high resolution and sensitivity of high-performance liquid chromatography using this dual approach has enabled the completion of greater than 95% of the sequence of P-component (M, 23,500) using less than 10 mg.

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Author

Jacqueline K. Anderson; John E. Mole

Publisher

Elsevier Science; Elsevier ; Elsevier Inc.; Elsevier BV (ISSN 0003-2697)

Published

1982

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)