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In situ assay of intracellular enzymes of yeast (Kluyveromyces fragilis) by digitonin permeabilization of cell membrane.

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Relation http://ir.cftri.com/2365/
AB-05-88
 
Title In situ assay of intracellular enzymes of yeast (Kluyveromyces fragilis) by digitonin permeabilization of cell membrane.
 
Creator Gowda, L. R.
Joshi, M. S.
Bhat, S. G.
 
Subject 19 Yeast
05 Enzymes
 
Description The yeast, Kluyveromyces fragilis was permeabilized to a number of low-molecular-weight substrates using digitonin. The activities of intracellular yeast enzymes, viz., alcohol dehydrogenase (ADH), beta-galactosidase, glucose-6-phosphate dehydrogenase, aspartase, and hexokinase were found to be much higher in the permeabilized cells than the untreated cells. The optimum conditions for permeabilization with reference to ADH were 0.1% digitonin at 37 degrees C for 15 min. The ADH activity in permeabilized cells was several-fold higher than that in cell free extracts prepared by either physical or chemical methods.
 
Date 1988
 
Type Article
PeerReviewed
 
Format application/pdf
 
Language en
 
Identifier http://ir.cftri.com/2365/1/Analytical_Biochemistry%2C_Volume_175%2C_Issue_2%2C_December_1988%2C_Pages_531-536.pdf
Gowda, L. R. and Joshi, M. S. and Bhat, S. G. (1988) In situ assay of intracellular enzymes of yeast (Kluyveromyces fragilis) by digitonin permeabilization of cell membrane. Analytical Biochemistry, 175 (2). pp. 531-6. ISSN 0003-2697