Literature DB >> 678547

Quantitative analysis of the amino-terminal residues of spectrin by use of the transamination reaction.

J R Hudson, G B Ralston.   

Abstract

The metal ion-catalysed transamination reaction has been examined as a means of quantitative amino-terminal analysis of proteins. Application of this method to the erythrocyte membrane protein, spectrin, showed that this protein contained a single amino-terminal residue per 240,000 daltons. This value supports the hypothesis that spectrin is comprised of two polypeptide chains of approx. 220,000 and 250,000 daltons, respectively.

Entities:  

Mesh:

Substances:

Year:  1978        PMID: 678547     DOI: 10.1016/0005-2795(78)90082-x

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


  2 in total

Review 1.  Spectrin: present status of a putative cyto-skeletal protein of the red cell membrane.

Authors:  V T Marchesi
Journal:  J Membr Biol       Date:  1979-12-14       Impact factor: 1.843

2.  Identification of proteolytically resistant domains of human erythrocyte spectrin.

Authors:  D W Speicher; J S Morrow; W J Knowles; V T Marchesi
Journal:  Proc Natl Acad Sci U S A       Date:  1980-10       Impact factor: 11.205

  2 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.