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Aminopeptidase N from Escherichia coli. Unusual interactions with the cell surface

European Journal of Biochemistry

Apr 15, 1977

M MurgierA Lazdunski

PMID: 323010

Abstract

The subcellular localization of aminopeptidase N (previously called aminoendopeptidase) has been investigated. This enzyme was found to be partially released (30-40%) by osmotic shock or by converting Escherichia coli K10 cells to spheroplasts. However, in all other E. coli strains (K12...read more

Mentioned in this Paper

GLB1
Alkalescens-Dispar Group
Protoplasm
Aminopeptidase
Alkaline Phosphatase
Spheroplasts
Electron Microscopy
ANPEP
Plasma Membrane
Galactosidase
Paper Details
References
  • References27
  • Citations14
123
  • References27
  • Citations14
12

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Aminopeptidase N from Escherichia coli. Unusual interactions with the cell surface

European Journal of Biochemistry

Apr 15, 1977

M MurgierA Lazdunski

PMID: 323010

DOI:

Abstract

The subcellular localization of aminopeptidase N (previously called aminoendopeptidase) has been investigated. This enzyme was found to be partially released (30-40%) by osmotic shock or by converting Escherichia coli K10 cells to spheroplasts. However, in all other E. coli strains (K12...read more

Mentioned in this Paper

GLB1
Alkalescens-Dispar Group
Protoplasm
Aminopeptidase
Alkaline Phosphatase
Spheroplasts
Electron Microscopy
ANPEP
Plasma Membrane
Galactosidase

Similar Papers Found In These Feeds

Solar-To-Chemical Conversion

This feed focuses on the latest research pertaining to mechanisms that facilitate reduction-oxidation biocatalysis only using light energy as a source. Here is the latest research.

Related Papers

European Journal of Biochemistry

Purification and properties of a periplasmic aminoendopeptidase from Escherichia coli

European Journal of BiochemistryDecember 15, 1975
C LazdunskiA Lazdunski
Paper Details
References
  • References27
  • Citations14
123
  • References27
  • Citations14
12
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