N-terminal groups of buffalo thyroglobulin.

ABSTRACT

N-Terminal analysis of purified buffalo thyroglobulin by the fluorodinitrobenzene method of Sanger yielded about 1.5 moles of DNP-glutamic acid per mole of buffalo thyroglobulin. No water-soluble DNP-amino acid was detectable as N-terminal. The presence of glutamic acid has been confirmed by Edman degradation and characterization of the PTH-amino acid in different solvent systems, and also after regeneration of free amino acid from PTH-amino acid in butanol-acetic acid-water (415, v/v) system. This is in contrast to the occurrence of aspartic acid or asparagine as N-terminals for several other mammalian thyroglobulins.