We have made preliminary designs of tandem mirror fusion reactors burning D-T fuel and of fusion-fission (hybrid) tandem mirrors producing both fissile fuel and electricity. For the hybrid reactor, we find that by using stream-stabilized, 2XIIB-like plugs and by injecting 200-keV deuterium beams into a tritium-plasma target confined electrostatically in the solenoid (two-component operation), we obtain a useful Q (fusion power/injection power) near unity. The D-T tandem reactor parameters are optimized to obtain the minimum capital cost per kW(e) net. For $200/kW(e) of 1200-keV neutral beam injection power in the plugs and a solenoid cost of about $3 million per metre length, the optimum Q is near 5. To allow for more expensive injector costs, a higher D-T reactor Q of 10 is obtainable with either increased power output or decreased neutron wall loading. Fokker--Planck calculations show steady-state Q approximately 5 for D-D tandem reactors burning only deuterium fuel and its reaction products, with most of the charged-particle fusion power recovered in a direct converter.

A Sarcina strain (Coccus P) produces two proteolytic enzymes. One is found only extracellularly, is far more prevalent, and is actively excreted during exponential growth. It is the enzyme responsible for the known strong proteolytic activity of the cultures of this strain. A second protease is, however, produced which remains associated with the intact cells but is released by the protoplasts. The two enzymes appear unrelated in their derivation. Calcium ions play an essential role in preventing autodigestion of the excreted enzyme. Bacterial proteins are found outside the cell boundary as a consequence either of passive processes such as leakage or lysis or of active excretion. Under conditions in which leakage and lysis do not occur, as during exponential growth, the cell boundary is a barrier causing a complete separation of the bulk of the intracellular proteins from the one or very few extracellular proteins, with no trace of either type being detectable on the wrong side of the boundary. Since in bacteria there is no evidence of protein being produced other than internally, the separation into intraand extracellular proteins should occur after peptide chain formation. The question arises as to whether the structure of the cell boundary or that …

It has been known that the extracellular proteinase of Coccus P is found only in cultures grown in the presence of Ca{sup 2+}. It is now shown that this cation is required neither for synthesis, excretion, or activation of a zymogen nor as a prosthetic factor necessary for enzymatic activity. The only function of Ca{sup 2+} is to stabilize the active structure of the enzyme molecule, presumably by substituting for absence of S-S bridges. In the absence of Ca{sup 2+} , the excreted proteinase undergoes rapid autodigestion and, instead of the active protein, its hydrolytic products are accumulated in the culture fluid. In minimal medium and under conditions of enzyme stability [presence of Ca{sup 2+} and Ficoll (Pharmacia)], Coccus P accumulates the proteinase at a gradually reduced speed although the rate of cultural growth remains constant. It is shown that this decline in rate of accumulation is caused by the excreted proteinase itself, possibly acting on its own precursor emerging from the cell in a form susceptible to proteolytic attack and not amenable to Ca{sup 2+} protection. A proteinase precursor is actually demonstrable in a calciumless culture at the onset of the enzyme accumulation which follows Ca{sup 2+} addition. It …