The authors have measured the asymmetry in the cross section for the reaction {gamma}p {yields} {pi}{sup +}n between the two stages of polarization of the initial proton normal to the plane of scattering. The initial laboratory photon energies, k, were 5 GeV and 16 GeV, and the regions of momentum transfer, t, covered were 0.14 {le} {radical}-t {le} 1.01 GeV/c and 0.14 {le} {radical}-t {le} 0.78 GeV/c respectively. A butanol polarized target was used with the SLAC 20 GeV/c magnetic spectrometer. The data show a sizeable asymmetry at both 5 GeV and 16 GeV. The 16 GeV data peak at {radical}-t {approx} 0.30 GeV/c with an asymmetry of about -0.70, and the 5 GeV data pak at {radical}-t {approx} 0.80 GeV/c with an asymmetry of about -0.70. The direction of our normal to the scattering plane is along (photon in) x (pion out).

The production of high energy (multi-GeV) proton beams by an electron ring accelerator is considered. Both the final energy and intensity of the proton beam depend on the choice of parameters for the electron ring. Possible sets of parameters, consistent with all the known requirements of ring stability, and which optimize the energy and (or) the intensity of the proton beam, are presented.

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 …