Thesis (Ph.D.)--Boston University / PLEASE NOTE: Boston University Libraries did not receive an Authorization To Manage form for this thesis or dissertation. It is therefore not openly accessible, though it may be available by request. If you are the author or principal advisor of this work and would like to request open access for it, please contact us at open-help@bu.edu. Thank you. / 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] / 2031-01-01
| Identifer | oai:union.ndltd.org:bu.edu/oai:open.bu.edu:2144/36791 |
| Date | January 1970 |
| Creators | Collins, John H. |
| Publisher | Boston University |
| Source Sets | Boston University |
| Language | en_US |
| Detected Language | English |
| Type | Thesis/Dissertation |
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