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Biomedical subjects

I G Wool

Publications and source records attributed to I G Wool.

At least 145 records · Page 8Linked to original sources
PubMed1974

The extraction of proteins from eukaryotic ribosomes and ribosomal subunits.

Proteins were extracted from rat liver ribosomes and ribosomal subunits: with 67% acetic acid (in the presence of 3.3 mM, 33 mM, or 67 mM Mg) with 2 M LiCL in 4 M urea; with 0.25 N HCI; with 1% SDS; and after RNase digestion. The most efficient extraction and the best recovery were either with acetic acid in the presence of 33 mM or 67 mM Mg, or with LiCI-urea. Protein extracted with acetic acid, LiCi-urea, or with HCI had little or no contamination with RNA. The ribosomal proteins were analyzed by two-dimensional polyacrylamide gel electrophoresis: the proteins extracted with acetic acid were the most soluble in the sample gel solution; their electrophoretograms displayed the maximum number of spots and the smallest number of derivatives or altered proteins. Preparations of protein extracted with SDS or RNase were relatively insoluble in the sample gel solution, and proteins extracted with HCI showed a large number of derivatives. All things considered, the most satisfactory method for the extraction of protein from eukaryotic ribosomes is with 67% acetic acid in the presence of 33 mM MgCl2.

Animals↗
PubMed1974

The identification of the eukaryotic ribosomal proteins homologous with Escherichia coli proteins L7 and L12.

Antibodies were raised against eukaryotic (rat liver) and prokaryotic (E. coli) ribosomal particles and ribosomal proteins. The antisera were characterized and used to determine the identity of the eukaryotic proteins homologous to E. coli L7 and L12. The large subunit of rat liver ribosomes contains two acidic proteins, L40 and L41; they migrate during two-dimensional polyacrylamide gel electrophoresis in a way that mimics the behavior of L7 and L12. Rat liver L40 and L41 were found to be immunologically related to E. coli L7/L12, hence the proteins are likely to share some structural homology.

Animals↗
PubMed1974

A kinase that transfers the gamma-phosphoryl group of GTP to proteins of eukaryotic 40S ribosomal subunits.

An enzyme in rat-liver cytosol transferred the gamma-phosphoryl of GTP to serine and threonine residues of at least four proteins (S6, S10, S14 or S15, and S17) of the small (40S) subunit of rat-liver ribosomes. A number of nonribosomal proteins in the enzyme preparation were also phosphorylated; they were preferentially and tightly bound to the large subunit. The enzyme could be distinguished from protein kinase-ATP (which also phosphorylated ribosomal proteins) by a number of criteria: (1) GTP was the phosphoryl donor; (2) the pattern of phosphorylation of ribosomal proteins by the two enzymes was different; and (3) the protein kinase that used GTP as the phosphoryl donor was not stimulated by cyclic AMP (or by cyclic GMP).

Adenosine Triphosphate↗