Search PubMed⌕ Search

Biomedical subjects

Y Kojima

Publications and source records attributed to Y Kojima.

At least 505 records · Page 28Linked to original sources
PubMed1979

Metallothionein: an exceptional metal thiolate protein.

Metallothioneins are unusual, low molecular weight proteins of extremely high sulphur and metabl content. They occur in substantial quantity and in multiple variant forms in parenchymatous tissues (liver, kidney, intestines) of vertebrates and certain microorganisms (Neurospora crassa, yeast). They are though to play a central role in the cellular metabolism of metals such as zinc, copper and cadmium. All mammalian forms studied are single chains with 20 cysteinyl residues among a total of 61 amino acid residues and highly characteristic amino acid sequences. Their most conspicuous common features are seven -Cys-X-Cys- sequences where X stands for an alphatic residue other than Cys. Together with additional cysteinyl residues located elsewhere in the chain and brought into juxtaposition by appropriate chain folding, these dithiol sequences are believed to form the basis of the trithiolate chelating structures typical of most of the six or seven metal-binding sites of the mammalian cadium- and/or zinc-containing metallothioneins. The positions of the cysteinyl residues are preserved in evolution: the copper-containing metallothionein from Neurospora crassa, containing only 25 amino acid residues, has a distribution of metal-binding cysteinyl residues identical to that of the N-terminal portion of the mammalian chains. The detailed physiological role of metallothionein remains to be clarified but its biosynthesis is known to be modulated by nutritional and endocrine factors. Recent evidence suggests that metallothionein is a critical determinant in the homeostasis of zinc.

Amino Acid Sequence↗
PubMed1979

Regions of the lipopolysaccharide of Pseudomonas aeruginosa essential for antitumor and interferon-inducing activities.

Resistance against ascites tumor development and interferon-inducing activity were demonstrated in lipopolysaccharide derived from the protein-lipopolysaccharide complex obtained from an autolysate of Pseudomonas aeruginosa. Lipid A obtained from the lipopolysaccharide was sufficient to induce interferon in vitro but no antitumor activity was found if lipid A or the polysaccharide derived from lipopolysaccharide was injected into the animal. Chemical modification of the polysaccharide portion or deacylation of the lipopolysaccharide also diminished antitumor activity. In contrast, interferon was induced by these incomplete lipopolysaccharides. These results indicate that both the lipid A portion and covalently linked polysaccharide are necessary for the inhibition of ascites tumor development, whereas incomplete lipid A with amide-linked fatty acids is sufficient to induce interferon in vitro.

Amino Acids↗