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Di-tertiarybutylnitroxide (DTBN), which they have tried to use as a trapping agent to identify the species giving rise to the photo-induced EPR signals in photosynthetic materials, functions as a Hill reagent with spinach chloroplasts. Evidence is presented which indicates that the reduction of DTBN is affected by photosystem II of the electron transport system of spinach chloroplasts. The reduced form of DTBN, the hydroxylamine, undergoes a photo-oxidation with spinach chloroplasts. Possible explanations of this apparent inconsistency are presented. A product which could be ascribed to a chemical coupling reaction between the nitroxide and the radical species giving rise to the photo-induced EPR signals in spinach chloroplasts was not detected, even using radioactive tracer methods.

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Static quadrupole moments of the first excited states of {sup 28}Si, {sup 32}S, and {sup 40}Ar have been measured using the reorientation effect in projectile Coulomb excitation. The results obtained are Q({sup 28}Si,2{sup +}) = +0.11 {+-} 0.05 b, Q({sup 32}S,2{sup +}) = -0.20 {+-} 0.06 b, and Q({sup 40}Ar, 2{sup +}) = +0.01 {+-} 0.04 b.

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Relationships necessary for ring stability are derived between the self-focusing forces of an electron ring and the magnetic field gradient defocusing forces present near and just subsequent to the start of ring acceleration.

A calculation is given of the radiated energy loss from a charged rod which moves at constant speed past an infinite set of parallel semi-infinite conducting plates of infinitesimal thickness, with the rod taken parallel to and at a fixed distance from the plate edges. The problem is analyzed using the Wiener-Hopf technique, and the resulting formulas are evaluated analytically in the limits of high rod speed and low rod speed, and compared with numerical evaluation over the full range of speeds.

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We discuss the possibility of using synchrotron radiation to form electron rings having a very high electric field to hold the ions inside the ring. The formulas describing bow the energy and the dimension of the ring change under the effect of synchrotron radiation are derived, and a numerical example is given.

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 …

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