Catalase-negative mutants of Escherichia coli

Efrat Meir; Ezra Yagil

doi:10.1007/BF01567569

Catalase-negative mutants of Escherichia coli

Efrat Meir, Ezra Yagil^*

^*Corresponding author for this work

Biochemistry Molecular Biology

Research output: Contribution to journal › Article › peer-review

Abstract

Catalase activity in crude extracts of Escherichia coli has two pH optima: one at pH 6.8 and the other at pH 10.5. The former is inducible by H₂O₂ and is the major species in exponential cells. The latter is constitutive and is the major species in stationary cells. Both activities are repressed by glucose. Catalase-negative mutants that are impaired in the pH-6.8 activity were isolated by the inability of aerobically grown mutagenized colonies to decompose H₂O₂. One mutant (cat2) characterized is hypersensitive to H₂O₂.

Original language	English
Pages (from-to)	13-17
Number of pages	5
Journal	Current Microbiology
Volume	11
Issue number	1
DOIs	https://doi.org/10.1007/BF01567569
State	Published - Jan 1984

Access to Document

10.1007/BF01567569

Cite this

@article{0c1c954a90b044ca819c60a3c5aa1344,

title = "Catalase-negative mutants of Escherichia coli",

abstract = "Catalase activity in crude extracts of Escherichia coli has two pH optima: one at pH 6.8 and the other at pH 10.5. The former is inducible by H2O2 and is the major species in exponential cells. The latter is constitutive and is the major species in stationary cells. Both activities are repressed by glucose. Catalase-negative mutants that are impaired in the pH-6.8 activity were isolated by the inability of aerobically grown mutagenized colonies to decompose H2O2. One mutant (cat2) characterized is hypersensitive to H2O2.",

author = "Efrat Meir and Ezra Yagil",

year = "1984",

month = jan,

doi = "10.1007/BF01567569",

language = "אנגלית",

volume = "11",

pages = "13--17",

journal = "Current Microbiology",

issn = "0343-8651",

publisher = "Springer New York",

number = "1",

}

TY - JOUR

T1 - Catalase-negative mutants of Escherichia coli

AU - Meir, Efrat

AU - Yagil, Ezra

PY - 1984/1

Y1 - 1984/1

N2 - Catalase activity in crude extracts of Escherichia coli has two pH optima: one at pH 6.8 and the other at pH 10.5. The former is inducible by H2O2 and is the major species in exponential cells. The latter is constitutive and is the major species in stationary cells. Both activities are repressed by glucose. Catalase-negative mutants that are impaired in the pH-6.8 activity were isolated by the inability of aerobically grown mutagenized colonies to decompose H2O2. One mutant (cat2) characterized is hypersensitive to H2O2.

AB - Catalase activity in crude extracts of Escherichia coli has two pH optima: one at pH 6.8 and the other at pH 10.5. The former is inducible by H2O2 and is the major species in exponential cells. The latter is constitutive and is the major species in stationary cells. Both activities are repressed by glucose. Catalase-negative mutants that are impaired in the pH-6.8 activity were isolated by the inability of aerobically grown mutagenized colonies to decompose H2O2. One mutant (cat2) characterized is hypersensitive to H2O2.

UR - http://www.scopus.com/inward/record.url?scp=0021175748&partnerID=8YFLogxK

U2 - 10.1007/BF01567569

DO - 10.1007/BF01567569

M3 - ???researchoutput.researchoutputtypes.contributiontojournal.article???

AN - SCOPUS:0021175748

SN - 0343-8651

VL - 11

SP - 13

EP - 17

JO - Current Microbiology

JF - Current Microbiology

IS - 1

ER -

Catalase-negative mutants of Escherichia coli

Abstract

Access to Document

Other files and links

Fingerprint

Cite this