Photoaffinity labeling of thiamin-binding component in yeast plasma membrane with [3H]4-azido-2-nitrobenzoylthiamin

FEBS Letters
H NishimuraA Iwashima


When prepared from Saccharomyces cerevisiae through an acid precipitation at pH 5.0 for a crude particulate fraction obtained by mechanical agitation of yeast protoplasts with glass beads, the plasma membranes have more remarkable binding quantities of [14C]thiamin (Kd, 51 nM; Bmax, 263 pmol per mg of protein) compared with our previously prepared membranes [(1986) Experientia 42, 607-608]. Photoaffinity labeling of these yeast plasma membranes with [3H]4-azido-2-nitrobenzoylthiamin resulted in the covalent modification of a membrane component with an apparent molecular mass of 6-8 kDa. The extent of its labeling was markedly decreased by previous addition of thiamin. This result suggests that the small membrane component (6-8 kDa) takes part in the thiamin binding of thiamin carrier protein(s) in yeast plasma membranes.


Dec 1, 1975·Biochimica Et Biophysica Acta·A IwashimaY Nose
Mar 27, 1979·Biochimica Et Biophysica Acta·A Iwashima, H Nishimura
Nov 2, 1979·Biochimica Et Biophysica Acta·A IwashimaY Nose
May 21, 1976·Biochimica Et Biophysica Acta·G F FuhrmannA P Theuvenet
Oct 1, 1988·Archives of Biochemistry and Biophysics·H NishimuraA Iwashima
Jun 15, 1986·Experientia·H NishimuraA Iwashima
Dec 13, 1973·Biochimica Et Biophysica Acta·A IwashimaY Nose

Related Concepts

Thiamine-binding protein
PHO3 protein, S cerevisiae
PHO5 protein, S cerevisiae
Acid Phosphatase
Affinity Labels
Carrier Proteins
Plasma Membrane

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