A 3-hydroxy-3-methylglutaryl-CoA lyase gene in the photosynthetic bacterium Rhodospirillum rubrum.

A 1.2 kb long DNA segment from Rhodospirillum rubrum has been sequenced (EMBL/GenBank accession number: U41280). This DNA segment includes the first sequenced gene for a putative 3-hydroxy-3-methylglutaryl-CoA (HMG-CoA) lyase, termed hmgL, from a photosynthetic organism.

Comparative studies of phosphoprotein preparations from rat incisor dentin.

Phosphoprotein was obtained from rat incisor dentin either by extraction at elevated ionic strength after acetic acid demineralization, or by extraction simultaneous with demineralization in neutral EDTA solution. Purification of solubilized proteins was achieved by Sepharose 4B and DEAE-cellulose chromatography. Polyacrylamide gel electrophoresis of the material from the two preparations resulted in one single band.

Simultaneous purification and some properties of aspartate: tRNA ligase and seven other amino-acid:tRNA ligases from Escherichia coli.

A procedure is described for the purification of the aspartate:tRNA ligase from Escherichia coli to a stage where it was homogeneous by polyacrylamide gel electrophoresis. From the same batch of E. coli the lysine, phenylalanine and serine ligases were obtained in an apparently homogeneous form while the alanine, glutamine, leucine and valine enzymes had a purity varying from 20% to 80%.