Literature DB >> 14060440

THE REVERSION OF CATALASE DURING GROWTH OF YEAST IN ANAEROBIOSIS.

J G KAPLAN.   

Abstract

Growth of originally aerobic bakers' yeast under conditions of anaerobiosis caused a decrease in the total specific catalatic activity (patent plus cryptic) of one-half per generation. It is concluded that reversion of catalase was a dilution, rather than a destruction, of the intracellular enzyme. However, the specific patent (whole cell) catalase activity remained constant for one or more generations, and then declined at a considerably slower rate than did the total activity. Thus the cryptic factor diminished progressively during anaerobic growth; after seven or eight generations virtually all the catalase was patent; i.e., the cryptic factor (the ratio of total enzyme to patent enzyme) was approximately unity. At this point, the basal level of enzyme was attained, and thereafter maintained by a basal synthesis, which produced only the patent, heat-stable, variety. Aerobic growth caused a significant, but much smaller, decline of both total catalase activity and of the cryptic factor. The data suggested that during reversion, the cryptic, heat-labile catalase became progressively converted to the patent, heat-resistant form. A model of these events is presented.

Entities:  

Keywords:  CATALASE; SACCHAROMYCES

Mesh:

Substances:

Year:  1963        PMID: 14060440      PMCID: PMC2195334          DOI: 10.1085/jgp.47.1.103

Source DB:  PubMed          Journal:  J Gen Physiol        ISSN: 0022-1295            Impact factor:   4.086


  9 in total

1.  On the mechanism of beta-galactosidase induction.

Authors:  B E WRIGHT; G McNEIL
Journal:  Arch Biochem Biophys       Date:  1961-11       Impact factor: 4.013

2.  The effect of inhibitors on the induction of cryptic and patent yeast catalase.

Authors:  J G KAPLAN
Journal:  Enzymologia       Date:  1963-05-15

3.  Catalase activity, sensitivity to hydrogen peroxide, and radiation response in the genus Escherichia.

Authors:  M S ENGEL; H I ADLER
Journal:  Radiat Res       Date:  1961-09       Impact factor: 2.841

4.  The components of maltozymase in yeast, and their behavior during deadaptation.

Authors:  J J ROBERTSON; H O HALVORSON
Journal:  J Bacteriol       Date:  1957-02       Impact factor: 3.490

5.  Induced biosynthesis of lysine decarboxylase in Bacterium cadaveris.

Authors:  J MANDELSTAM
Journal:  J Gen Microbiol       Date:  1954-12

6.  Enzymatic deadaptation.

Authors:  H V RICKENBERG; C YANOFSKY; D M BONNER
Journal:  J Bacteriol       Date:  1953-12       Impact factor: 3.490

7.  The alteration of intracellular enzymes. III. The effect of temperature on the kinetics of altered and unaltered yeast catalase.

Authors:  M J FRASER; J G KAPLAN
Journal:  J Gen Physiol       Date:  1955-03-20       Impact factor: 4.086

8.  Interactions between enzyme-forming systems during adaptation.

Authors:  S SPIEGELMAN; R DUNN
Journal:  J Gen Physiol       Date:  1947-11-20       Impact factor: 4.086

9.  The alteration of intracellular enzymes. II. The relation between the surface and the biological activities of altering agents.

Authors:  J G KAPLAN
Journal:  J Gen Physiol       Date:  1954-11-20       Impact factor: 4.086

  9 in total
  4 in total

1.  [The effect of ascorbic acid on catalase induction in microorganism cultures].

Authors:  H H Mazarean; E Kovács
Journal:  Experientia       Date:  1965-09-15

2.  AN INDUCIBLE SYSTEM FOR THE HYDROLYSIS AND TRANSPORT OF BETA-GLUCOSIDES IN YEAST. I. CHARACTERISTICS OF THE BETA-GLUCOSIDASE ACTIVITY OF INTACT AND OF LYSED CELLS.

Authors:  J G KAPLAN
Journal:  J Gen Physiol       Date:  1965-05       Impact factor: 4.086

3.  Effect of mercurial compounds on structure-linked latency of lysosomal hydrolases.

Authors:  M A Verity; A Reith
Journal:  Biochem J       Date:  1967-11       Impact factor: 3.857

4.  The beta-glucosidase of the yeast cell surface.

Authors:  J G Kaplan; W Tacreiter
Journal:  J Gen Physiol       Date:  1966-09       Impact factor: 4.086

  4 in total

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