Literature DB >> 4552687

A mutationally altered alkaline phosphatase from Escherichia coli. I. Formation of an active enzyme in vitro and phenotypic suppression in vivo.

S E Halford, D A Lennette, P M Kelley, M J Schlesinger.   

Abstract

Entities:  

Mesh:

Substances:

Year:  1972        PMID: 4552687

Source DB:  PubMed          Journal:  J Biol Chem        ISSN: 0021-9258            Impact factor:   5.157


× No keyword cloud information.
  3 in total

1.  Localization of polyribosomes containing alkaline phosphatase nascent polypeptides on membranes of Escherichia coli.

Authors:  R Cancedda; M J Schlesinger
Journal:  J Bacteriol       Date:  1974-01       Impact factor: 3.490

2.  Mutationally altered rate constants in the mechanism of alkaline phosphatase.

Authors:  S E Halford; M J Schlesinger
Journal:  Biochem J       Date:  1974-09       Impact factor: 3.857

3.  Fluorotyrosine alkaline phosphatase from Escherichia coli: preparation, properties, and fluorine-19 nuclear magnetic resonance spectrum.

Authors:  B D Sykes; H I Weingarten; M J Schlesinger
Journal:  Proc Natl Acad Sci U S A       Date:  1974-02       Impact factor: 11.205

  3 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.