title: 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 (4:1:5, v/v) system. This is in contrast to the occurrence of aspartic acid or asparagine as N-terminals for several other mammalian thyroglobulins.
authors.affiliation: Department of Biochemistry, Osmania University, Hyderabad.
authors.forename: V
authors.initials: V
authors.lastname: Deshpande
authors.forename: L K
authors.initials: LK
authors.lastname: Ramachandran
mesh_terms: D000596:Amino Acids / Q000032:analysis*; D000818:Animals; D002020:Buffaloes; D013954:Thyroglobulin / Q000032:analysis*
chemical_list: D000596:Amino Acids; D013954:Thyroglobulin