Structural studies on alpha1-acid glycoprotein
Collins, John H.
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A carbohydrate-free peptide was isolated from a tryptic digest of trifluoroacetylated alpha1-acid glycoprotein (AG) in a yield of 0.9 moles per 44,000 gms. of protein. The purity was established by electrophoresis and chromatography, and the amino acid sequence determined to be: (-Tfa-Lys-Gln-Glu-Glu-Gly-Glu-Ser. The high yield indicated that it was a primary tryptic peptide, yet it did not possess a C-terminal arginine. Since it had been previously shown that AG has serine as its C-terminal residue, it is proposed that the peptide represents the C-terminus of the protein. During the course of this work, more than 100 amino acid analyses were required. An automated ion-exchange type analyzer was not available, and an alternative procedure had to be devised. A system combining quantitative high-voltage electrophoresis and gas-liquid chromatography was standardized and used for almost all of the required analyses. The system proved to be satisfactory for the peptides that were isolated. [TRUNCATED]
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