The effect of amino acid analogues on alkaline phosphatase formation in Escherichia coli K-12. IV. Substitution of canavanine for arginine.
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In a histidine auxotroph of Escherichia coli, the replacement of histidine by 2-methylhistidine during protein synthesis completely prevented the formation of active alkaline phosphatase.About:
This article is published in Journal of Biological Chemistry.The article was published on 1969-07-25 and is currently open access. It has received 58 citations till now. The article focuses on the topics: Canavanine & Alkaline phosphatase.read more
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Journal ArticleDOI
The effect of amino acid analogues and heat shock on gene expression in chicken embryo fibroblasts.
TL;DR: Several laboratories have reported synthesis of proteins with similar molecular weights in cells subjected to conditions that alter glucose metabolism, and it is speculated that these proteins may be associated with a hexose transport system.
Journal ArticleDOI
The Biological Effects and Mode of Action of L-Canavanine, a Structural Analogue of L-Arginine
TL;DR: Canavanine is a highly toxic secondary plant constituent that probably functions as an allelochemic agent that deters the feeding activity of phytophagous insects and other herbivores.
Journal ArticleDOI
An Expanded Set of Amino Acid Analogs for the Ribosomal Translation of Unnatural Peptides
TL;DR: It is shown that over 50 unnatural amino acids can be incorporated into peptides by ribosomal translation, and these building blocks provide new opportunities for in vitro selections with highly modified drug-like peptides.
Book ChapterDOI
17 E. coli Alkaline Phosphatase
Ted W. Reid,Irwin B. Wilson +1 more
TL;DR: In this article, the molecular properties and catalytic properties of E. coli alkaline phosphatase were discussed and Levinthal concluded that all of the isozymes were coded for by the same gene.
Journal ArticleDOI
A Novel Means for Dealing with L-Canavanine, a Toxic Metabolite
TL;DR: L-canavanine is a highly toxic L-arginine analog found in some leguminous seeds, but larvae of the bruchid beetle Caryedes brasiliensis subsist solely on tissues of the mature seed of Dioclea megacarpa, which contains more than 8 percent L- canavanine by dry weight.
References
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Journal ArticleDOI
A Method for Determining the Sedimentation Behavior of Enzymes: Application to Protein Mixtures
Robert G. Martin,Bruce N. Ames +1 more
TL;DR: Sucrose gradient centrifugation is found to be a suitable method for determining sedimentation coefficients of enzymes in protein mixtures and the sedimentation behavior of several of the enzymes in the pathway of histidine biosynthesis in S. typhimurium has been determined.
Journal ArticleDOI
The release of enzymes from Escherichia coli by osmotic shock and during the formation of spheroplasts.
Harold C. Neu,Leon A. Heppel +1 more
TL;DR: A new method for releasing most of the inducible alkaline phosphatases and of the cyclic phosphodiesterase in high yield without greatly impairing the viability of the cells is developed.
Journal ArticleDOI
A fine-structure genetic and chemical study of the enzyme alkaline phosphatase of E. Coli I. Purification and characterization of alkaline phosphatase
A. Garen,C. Levinthal +1 more
TL;DR: A procedure for purification of alkaline phosphatase from E. coli is described, and several physical-chemical propetiies of the purified enzyme are reported.
Journal Article
A modification of the colorimetric phosphorus determination for use with the photoelectric colorimeter.
Journal ArticleDOI
Alkylation and identification of the histidine residues at the active site of ribonuclease.
TL;DR: The present communication is concerned with theracterization of the two products of the reaction, the establishment of the position of the amino acid residues altered in each instance, and the determination of which of theTwo structural isomers is formed when a given imidazole ring in ribonuclease is alkylated by iodoacetate.