Literature DB >> 7115740

The isoelectric focusing of human thyroglobulin.

C Davoli, S Grimaldi, G Rusca, M Andreoli, H Edelhoch.   

Abstract

The isoelectric focusing of human thyroglobulin has been studied on slab gels. Three bands, focusing between pH 4.4 and 4.7, are observed. Deglycosylation of thyroglobulin does not affect the distribution of focused bands, but increases the pH range of focusing slightly. Native thyroglobulin and its half-sized subunit show the same distribution of isoelectric bands. Refocusing of one band results in the appearance of the three original bands. It appears that soluble complexes of thyroglobulin with ampholyte account for the apparent heterogeneity observed on isoelectric focusing.

Entities:  

Mesh:

Substances:

Year:  1982        PMID: 7115740     DOI: 10.1016/0167-4838(82)90184-4

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  2 in total

1.  Antigenic determinants of human thyroglobulin differentiated using antigen fragments.

Authors:  D K Male; B R Champion; G Pryce; H Matthews; P Shepherd
Journal:  Immunology       Date:  1985-03       Impact factor: 7.397

2.  A new polymorphism of thyroxin-binding globulin in three African groups (Mali) with endemic nodular goitre.

Authors:  J Constans; M T Ribouchon; C Gouaillard; A Chaventré; J Clayton
Journal:  Hum Genet       Date:  1992-05       Impact factor: 4.132

  2 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.