Electron and nuclear pressures in electron-nucleus mixtures

It is shown for an electron-nucleus mixture that the electron and nuclear pressures are defined clearly and simply by the virial theorem; the total pressure of this system is a sum of these two pressures. The electron pressure is different from the conventional electron pressure being expressed as the sum of two times of kinetic energy and the potential energy in that the nuclear virial term is subtracted; this fact is exemplified by several kinds of definitions for the electron pressure enumerated in this work. The conventional definition of the electron pressure in terms of the nuclear virial term is shown inappropriate. Similar remarks are made about the definition of the stress tensor in this mixture. It is also demonstrated that both of the electron and nuclear pressures become zero at the same time for a metal in the vacuum, in contrast to the conventional viewpoint that the zero pressure is realized by a result of the cancellation between the electron and nuclear pressures, each of which is not zero. On the basis of these facts, a simple equation of states for liquid metals is derived, and examined numerically for liquid alkaline metals by use of the quantum hypernetted chain equation and the Ashcroft model potential.Comment: 24pages. 2 ps-figures, use epsf.sty, namelist.sty,REVtex macro

The Spoken Language Program Of The Army Japanese Language School At The University Of Michigan 1

Peer Reviewedhttp://deepblue.lib.umich.edu/bitstream/2027.42/98238/1/j.1467-1770.1948.tb00876.x.pd

A Check‐List Of Tests For Various Types Of Proficiency In A Foreign Language

Peer Reviewedhttp://deepblue.lib.umich.edu/bitstream/2027.42/98230/1/j.1467-1770.1956.tb01206.x.pd

A Cooperative Program in Chinese and Japanese

Peer Reviewedhttp://deepblue.lib.umich.edu/bitstream/2027.42/98147/1/j.1467-1770.1963.tb01278.x.pd

Cytotoxicity of the Bacillus thuringiensis Crystal Protein against Mammalian Cells

The crystal proteins produced by Bacillus thuringiensis subsp, israelensis (Bti) and subsp. coreanensis A1519 strain were examined for the cytotoxicity against MOLT-4 and HeLa cells by MTT assay and LDH assay, The A1519 crystal proteins processed by proteinase K exhibited the specific cell-killing activity toward MOLT-4 with little damage to the cell membrane, On the other hand, the Bti crystal proteins processed by proteinase K caused the substantial damage to the cell membrane of both MOLT-4 and HeLa, leading to the cell lysis. The non-digested crystal proteins of both strains exhibited no cytotoxicity, These data suggested that while the Bti crystal proteins caused the colloid-osmotic swelling and cell lysis of MOLT-4 and HeLa, the proteinase K-digested A1519 crystal proteins induced the specific cell death of MOLT-4 through a mechanism other than that of Bti

The role of interhelical cleavage for insecticidal activityof Bacillus thuringiensis Cry4A toxin

The Cry4A toxin is a dipteran-specific insecticidal protein produced by Bacillus thuringiensis subsp. israelensis as a protoxin of 130 kDa. Its active form is a heterodimer of 20- and 45-kDa fragments which is generated by an interhelical cleavage of a 60-kDa intermediate at the position of Gln236 between α5 and α6 helices in domain I. On the other hand, Cry1Aa, which is also produced as a 130-kDa protoxin but toxic to lepidopteran larvae, was processed into the active 60-kDa fragment with no additional cleavage. To investigate the role of the intramolecular cleavage of Cry4A for its insecticidal activity, the loop between α5 and α6 of Cry4A which includes the cleavage site was substituted for the corresponding region of Cry1Aa. The resulting mutant designated GST-60Loop was expressed as a GST-fusion protein. A difference of the processing profile was observed between GST-60 and GST-60Loop in the in vitro digestion assay by trypsin, and the insecticidal activity of GST-60Loop was two-fold lower than that of GST-60. These results suggested that the interhelical cleavage of Cry4A promoted the toxicity against C. pipiens larvae

The role of helices of domain I for the insecticidal activity of Bacillus thuringiensis Cry4A toxin

An active form of Cry4A is a heterodimer of the 20- and 45-kDa fragments that are derived from the 130-kDa Cry4A protoxin. To investigate the function of these two fragments, several deletion mutants were constructed and expressed in E.coli as the GST (glutathione-S-transferase) fusion proteins. The results of the bioassay against Culex pipiens larvae showed that the interaction of two fragments of Cry4A was necessary for the toxicity, and that the C-terminal 67 amino acids of the 20-kDa fragment corresponding to the helices α4 and α5 were involved in determining the insecticidal activity. Surprisingly the lack of helix α5 did not affect the toxicity to C. pipiens, suggesting that the role of helix α5 of Cry4A was different from that postulated in the case of Cry4A toxins