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Open AccessJournal ArticleDOI

The two subunits of penicillin acylase are processed from a common precursor

TLDR
In this paper, les deux sous-unites de la penicilline acylase d'Escherichia coli proviennent d'un precurseur commun polypeptidique localise exclusivement dans la membrane.
Abstract
Les resultats montrent que les deux sous-unites de la penicilline acylase d'Escherichia coli proviennent d'un precurseur commun polypeptidique localise exclusivement dans la membrane

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Molecular Regulation of β-Lactam Biosynthesis in Filamentous Fungi

TL;DR: A comparison with the regulatory mechanisms (regulatory proteins and DNA elements) involved in the regulation of genes of primary metabolism in lower eukaryotes is thus of great interest and can be expected to have a major impact on rational strain improvement programs.
Journal ArticleDOI

Cloning and characterization of the genes for two distinct cephalosporin acylases from a Pseudomonas strain.

TL;DR: A DNA library of this strain was constructed in Escherichia coli and screened for the ability to deacylate GL-7ACA to 7ACA, and the acyII-encoded enzyme was found to yield 7ACA from cephalosporin C by direct deacylation.
Journal ArticleDOI

Polycistronic Viral Vectors

TL;DR: The description and comparison of the strategies for co-expression of two genes in bicistronic vectors, from the oldest to the more recently described, and a classification of these strategies based upon either the use of multiple transcripts (with transcriptional mechanisms), or single transcripts (using translational/post-translational mechanisms).
Journal ArticleDOI

The role of penicillin amidases in nature and in industry

TL;DR: Clues to the biological role of this enzyme have been provided, as well as new strategies for the commercial production and utilization of PA, revealing a variety of interesting features that are unique among microorganisms.
References
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Journal ArticleDOI

Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4

TL;DR: Using an improved method of gel electrophoresis, many hitherto unknown proteins have been found in bacteriophage T4 and some of these have been identified with specific gene products.
Journal Article

Cleavage of structural proteins during the assemble of the head of bacterio-phage T4

U. K. Laemmli
- 01 Jan 1970 - 
TL;DR: Using an improved method of gel electrophoresis, many hitherto unknown proteins have been found in bacteriophage T4 and some of these have been identified with specific gene products as mentioned in this paper.
Journal ArticleDOI

Peptide mapping by limited proteolysis in sodium dodecyl sulfate and analysis by gel electrophoresis.

TL;DR: A rapid and convenient method for peptide mapping of proteins has been developed that involves partial enzymatic proteolysis in the presence of sodium dodecyl sulfate and analysis of the cleavage products by polyacrylamide gel electrophoresis.
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