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Biomedical subjects

Y Hatefi

Publications and source records attributed to Y Hatefi.

161 records · Page 9Linked to original sources
PubMed1971

Glucosylation of teichoic acid: solubilization and partial characterization of the uridine diphosphoglucose: polyglycerolteichoic acid glucosyl transferase from membranes of Bacillus subtilis.

Polyglycerolteichoic acid:glucosyl transferase (TAG transferase), one of the three enzymes involved in the pathway leading to the glucosylation of teichoic acid in Bacillus subtilis 168, was investigated. During the early stages of the growth of B. subtilis, TAG transferase is predominantly a soluble enzyme found in the cytoplasm. As growth proceeds, the amount of soluble enzyme decreases and the proportion of insoluble, membrane-bound TAG transferase increases, reaching a maximal value at the close of the logarithmic phase. Data are presented which suggest that these are two forms of the same enzyme, or have some common component. The effects of chaotropic agents, such as sodium trichloroacetate and sodium perchlorate, on the cytoplasmic membrane were also studied. These data show that such compounds can effectively remove the TAG transferase from the membrane in a water-soluble form. A study of some of the physical properties of this solubilized enzyme suggests that there is little difference between the two forms of the enzyme. Experiments are described which indicate that the glucosyl transfer by both the membrane-bound and soluble enzymes is not mediated by lipids.

Bacillus subtilis↗
PubMed1969

Solubilization of particulate proteins and nonelectrolytes by chaotropic agents.

Chaotropic ions (those ions which favor the transfer of apolar groups to water) provide a highly effective means for the resolution of membranes and multicomponent enzymes and for increasing the water solubility of particular proteins and nonelectrolytes. The action of chaotropic agents is related to their effect on the structure and lipophilicity of water.

Cell Membrane↗
PubMedDate not supplied

Six unidentified reading frames of human mitochondrial DNA encode components of the respiratory-chain NADH dehydrogenase.

The products of six unidentified reading frames of human mitochondrial DNA are precipitated from a mitochondrial lysate by antibodies against highly purified native beef heart NADH-ubiquinone oxidoreductase (complex I). These products are enriched greatly in a human submitochondrial fraction enriched in NADH-Q1 and NADH-K3Fe(CN)6 oxidoreductase activities. We conclude that the six reading frames encode components of the respiratory-chain NADH dehydrogenase.

Animals↗