Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Isolation of Serratia marcescens mutants which could overproduce and excrete Escherichia coli alkaline phosphatase and beta-lactamase.

Archives of microbiology - 1 Jan 1994

Asdornnithee S, Akiyama K, Takata R

Abstract excerpt

Serratia marcescens mutants, which excrete Escherichia coli alkaline phosphatase (APase) encoded by the plasmid-bearing phoA gene, were isolated after mutagenesis by N-methyl-N'-nitro-N-nitrosoguanidine. These mutants produced two to four times as much APase as did the parent strain under a phosphate-limiting condition, and more than 70% of the enzyme was released into the culture medium. In addition,...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Alkaline Phosphatase
Share to beta-Lactamases
Share to Escherichia coli

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Mutation

Share to Plasmids

Share to Serratia marcescens

Share to Transformation, Bacterial

Source

Identifiers

PMID: 8042904
DOI: 10.1007/BF00288952

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Isolation of Serratia marcescens mutants which could overproduce and excrete Escherichia coli alkaline phosphatase and beta-lactamase.PMID 8042904Read ↗

[Biogenesis and secretion of alkaline phosphatase and its mutants in Escherichia coli. III. Substitution of N-terminal amino acids of alkaline phosphatase affect its biogenesis].Semantic proximity Read ↗

The molecular evolution of bacterial alkaline phosphatase: correlating variation among enteric bacteria to experimental manipulations of the protein.Semantic proximity Read ↗

Stable polyphosphate accumulation by a pseudo-revertant of an Escherichia coli phoU mutant.Semantic proximity Read ↗

[Isolation of Serratia marcescens mutants superproducers of endonuclease by exposure to nitrosomethylurea in a synchronized culture].Semantic proximity Read ↗

[Effect of Mutations in Extracellular Nuclease on the Characteristics of the Pigmented and Nonpigmented Serratia marcescens Strains].Semantic proximity Read ↗

[Isolation and certain properties of mutant alkaline phosphatase of Escherichia coli].Semantic proximity Read ↗

Physiological and biochemical analysis of the effects of alkaline phosphatase overproduction in Escherichia coli.Semantic proximity Read ↗

Growth depression of Serratia marcescens by plasmids that belong to incompatibility group P.Semantic proximity Read ↗

Biosynthesis of endochitinase of Serratia marcescens.Semantic proximity Read ↗

Isolation of behavioral mutants of Azospirillum brasilense by using Tn5 lacZ.Semantic proximity Read ↗

Accumulation of inorganic polyphosphate in phoU mutants of Escherichia coli and Synechocystis sp. strain PCC6803.Semantic proximity Read ↗

The metalloprotease gene of Serratia marcescens strain SM6.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.