N-terminal groups of buffalo thyroglobulin.

dc.contributor.authorDeshpande, Ven_US
dc.contributor.authorRamachandran, L Ken_US
dc.date.accessioned1990-04-01en_US
dc.date.accessioned2009-05-27T09:05:10Z
dc.date.available1990-04-01en_US
dc.date.available2009-05-27T09:05:10Z
dc.date.issued1990-04-01en_US
dc.description.abstractN-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.en_US
dc.description.affiliationDepartment of Biochemistry, Osmania University, Hyderabad.en_US
dc.identifier.citationDeshpande V, Ramachandran LK. N-terminal groups of buffalo thyroglobulin. Indian Journal of Biochemistry & Biophysics. 1990 Apr; 27(2): 118-20en_US
dc.identifier.urihttps://imsear.searo.who.int/handle/123456789/26402
dc.language.isoengen_US
dc.source.urihttps://https://www.niscair.res.in/ScienceCommunication/ResearchJournals/rejour/ijbb/ijbb0.aspen_US
dc.subject.meshAmino Acids --analysisen_US
dc.subject.meshAnimalsen_US
dc.subject.meshBuffaloesen_US
dc.subject.meshThyroglobulin --analysisen_US
dc.titleN-terminal groups of buffalo thyroglobulin.en_US
dc.typeJournal Articleen_US
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