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Journal ArticleDOI

Penicillin acylase extraction by osmotic shock

TLDR
Penicillin acylase was extracted from E. Coli by osmotic shock by factorial design, scaled up and integrated to a purification process in order to compare it with purification processes reported in the literature.
About
This article is published in Process Biochemistry.The article was published on 1992-07-01. It has received 22 citations till now. The article focuses on the topics: Penicillin amidase.

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Citations
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Journal ArticleDOI

Direct comparison between ion-exchange chromatography and aqueous two-phase processes for the partial purification of penicillin acylase produced by E. coli

TL;DR: It is clear that the results reported herein raise the consideration for the potential substitution of the chromatography process for PA recovery from E. coli as a first step for the development of an optimised and economic process with evident commercial application.
Journal ArticleDOI

Biotechnological advances on penicillin G acylase: pharmaceutical implications, unique expression mechanism and production strategies.

TL;DR: A state-of-the-art review in recent biotechnological advances associated with PGA, particularly in the production technologies with an emphasis on using the Escherichia coli expression platform.
Journal ArticleDOI

Penicillin acylase release from Escherichia coli cells by mechanical cell disruption and permeabilization

TL;DR: The high purity of the penicillin acylase was a consequence of the optimized differential enzyme release method which was validated by SDS gel electrophoresis.
Journal ArticleDOI

Ni(II)-based immobilized metal ion affinity chromatography of recombinant human prolactin from periplasmic Escherichia coli extracts.

TL;DR: A novel, two-step preparative technique is described for the purification of authentic recombinant human prolactin secreted into the periplasm of transformed Escherichia coli cells, leading to 77% recovery and superior resolution and yield than established ion-exchange chromatography.
Journal ArticleDOI

The relative importance of intracellular proteolysis and transport on the yield of the periplasmic enzyme penicillin amidase in Escherichia coli

TL;DR: Evidence is presented that the active enzyme is localized in the periplasmic space and maturation of pro-enzyme occurs during transport through the cytoplasmic membrane or rapidly after its entrance in theperiplasm.
References
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Journal Article

Protein Measurement with the Folin Phenol Reagent

TL;DR: Procedures are described for measuring protein in solution or after precipitation with acids or other agents, and for the determination of as little as 0.2 gamma of protein.
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.
Book ChapterDOI

On the Experimental Attainment of Optimum Conditions

TL;DR: The work described in this article is the result of a study extending over the past few years by a chemist and a statistician, which has come about mainly in answer to problems of determining optimum conditions in chemical investigations, but they believe that the methods will be of value in other fields where experimentation is sequential and the error fairly small.
Journal ArticleDOI

Simple, rapid, and quantitative release of periplasmic proteins by chloroform.

TL;DR: This method makes practical the analysis of the periplasmic protein complement of a large number of strains by treating cells with chloroform, and all the amino acid-binding proteins tested maintained their activity during chloro Form treatment.
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