Soyabean saponins. IX. Studies of their effect on birds, mammals and cold-blooded organisms.
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Biomedical subjects
Publications and source records attributed to A Bondi.
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Lysine biosynthesis in Staphylococcus aureus has been studied by use of a series of lysine auxotrophs. The strains were isolated after chemical mutagenesis. The majority of these mutant strains were classified according to the enzymatic step found to be deficient. Specific enzyme assays as well as nutritional tests were used to group the organisms. The enzymes included were dihydrodipicolinate synthetase, dihydrodipicolinate reductase, diaminopimelate epimerase, and diaminopimelate decarboxylase. The accumulation of diaminopimelate in certain mutants and the demonstration of dihydrodipicolinate synthetase and reductase provide the first detailed evidence that S. aureus utilizes the diaminopimelate pathway for lysine biosynthesis. A cell-free system was used to study the regulation of these enzymes with the exception of diaminopimelate epimerase. Lysine repressed all of the enzymes tested. The repression appeared to be coordinate in nature. The data presented provide suggestive evidence that the lysine biosynthetic region in S. aureus constitutes an operon.
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Williams, Daniel H., III (Hahnemann Medical College, Philadelphia, Pa.), A. Bondi, A. G. Moat, and F. Ahmad. Thermostability of Bacillus cereus penicillinase. J. Bacteriol. 91:257-261. 1966.-The extracellular penicillinase of Bacillus cereus, strain 13-10, exhibited an unusual thermostability. Whereas it was completely and irreversibly inactivated by heating at 70 C, it retained considerable activity when heated at 100 C for 30 min. The active enzyme remaining was completely stable to further heating at temperatures from 40 to 100 C for as long as 1 hr. Preparations of the enzyme heated to 100 C possessed pH (7.0) and temperature (37 C) optima identical with the unheated enzyme. Furthermore, both enzyme preparations exhibited identical combining capacity for the substrate (penicillin G), suggesting that the two preparations had similar hydrolytic properties. Our findings suggest that heating of penicillinase at 100 C results in the formation of a protein complex which is resistant to further denaturation by heat and other agents. Addition of certain metal ions to the enzyme solution before heat treatment increased the stability to heat at 100 C by virtue of their ability to induce complex formation. Pectin was shown to decrease thermostability, presumably by preventing aggregation of proteins present in the enzyme preparations. The well-known stabilizing effect of gelatin may be attributed to its role in enhancing complex formation.
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The utility of bioelectric impedance analysis was assessed for longitudinal evaluation of body composition in two groups of uremic patients, one on CAPD and one on hemodialysis treatment, with no clinical marks of hyperhydration or infection. Nineteen CAPD patients (11 men 8 women) and 21 HD patients (12 men 9 women) were studied with bioelectric impedance analysis for a period of 12 months; total body water, fat free mass, and fat mass were calculated from bioelectric impedance analysis data of resistance and reactance at time 0 and 12 months later. No significant differences in body composition were found in the two groups at time 0 and 12 months later, with a similar trend for total body water, fat free mass, and fat mass. In CAPD, a significant increase in body weight was observed due mainly to a rise in fat mass, particularly evident in women with uremia. Bioelectric impedance analysis appears to be an instrument easily repeatable and reliable in CAPD and HD patients, reflecting at the same time body composition, the dialytic adequacy of a technique, and the patient's well being.
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