Literature DB >> 371687

Isolation of a thiamine-binding protein from Saccharomyces cerevisiae.

A Iwashima, H Nishimura.   

Abstract

Thiamine-binding protein was isolated from Saccharomyces cerevisiae by successive procedures of cold osmotic shock treatment, DEAE-cellulose chromatography and ultrafiltration. The purified thiamine-binding protein was an electrophoretically homogeneous molecule which appeared to be a glycoprotein with a molecular weight of 140 000 by sodium dodecyl sulfate polyacrylamide gel electrophoresis. No thiamine-binding protein was observed by disc gel electrophoresis in the shock fluid released from yeast cells grown in the presence of 1 muM thiamine, indicating that the formation of this protein is regulated by exogenous thiamine as previously suggested.

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Year:  1979        PMID: 371687     DOI: 10.1016/0005-2795(79)90023-0

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


  3 in total

1.  A constitutive thiamine metabolism mutation, thi80, causing reduced thiamine pyrophosphokinase activity in Saccharomyces cerevisiae.

Authors:  H Nishimura; Y Kawasaki; K Nosaka; Y Kaneko; A Iwashima
Journal:  J Bacteriol       Date:  1991-04       Impact factor: 3.490

2.  Molecular docking of thiamine reveals similarity in binding properties between the prion protein and other thiamine-binding proteins.

Authors:  Nataraj S Pagadala; Trent C Bjorndahl; Nikolay Blinov; Andriy Kovalenko; David S Wishart
Journal:  J Mol Model       Date:  2013-10-15       Impact factor: 1.810

3.  Thiamine-binding activity of Saccharomyces cerevisiae plasma membrane.

Authors:  H Nishimura; K Nosaka; K Sempuku; A Iwashima
Journal:  Experientia       Date:  1986-06-15
  3 in total

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