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IN VIVO STUDIES OF RADIATION POTENTIATON BY IODOACETAMIDE AND OBSERVATIONS ON TUMOR TRANSPLANTATION IMMUNITY

Description: Iodoacetamide has been shown by others to be a radiation sensitizer for bacteria and for certain mammalian cells tested in vitro. This work describes an examination of the effectiveness of iodoacetamide used in vivo. Survival of ascites tumor cells maintained in the peritoneal cavity of mice was used as an indicator of sensitization. Survival was assessed using TD{sub 50} and total tumor cell population determination methods. A comparison of results obtained by these methods is made. The effect… more
Date: October 1, 1970
Creator: Richards, F. Robert & Kelly, Lola S.
Partner: UNT Libraries Government Documents Department
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Mechanism of Excretion of a Bacterial Proteinase: Demonstration of Two Proteolytic Enzymes Produced by a Sarcina Strain (Coccus P)

Description: 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 preventi… more
Date: June 29, 1970
Creator: Sarner, Nitza Z.; Bissel, Mina J.; Girolamo, Mario Di & Gorini, Luigi
Partner: UNT Libraries Government Documents Department
open access

Mechanism of Excretion of a Bacterial Proteinase: Factors Controlling Accumulation of the Extracellular Proteinase of a Sarcina Strain (Coccus P)

Description: 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 un… more
Date: June 29, 1970
Creator: Bissell, Mina J.; Tosi, Roberto & Gorini, Luigi
Partner: UNT Libraries Government Documents Department
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