Stability of penicillin in solutions of ephedrine
โ Scribed by Seeberg, Victor P. ;Brown, Doris Jane ;Johnson, Frederick F.
- Publisher
- Elsevier
- Year
- 1946
- Weight
- 251 KB
- Volume
- 35
- Category
- Article
- ISSN
- 0095-9553
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โฆ Synopsis
The stability of penicillin i n solutions of ephedrine has been determined. At refrigerator temperatures the stability of penicillin is not appreciably affected by ephedrine. At room and incubator temperatures ephedrine exerts an appreciable effect on the stability of penicillin in some preparations. This effect is greatest o n crystalline sodium penicillin and commercial calcium penicillin and least when commercial sodium penicillin is used.
N TREATING conditions of sphenoethmoiditis with penicillin, relief of nasal congestion by the use of a local vasoconstrictor such as ephedrine has been recommended by Woodward and Holt (1) in order to allow the penicillin to come in contact with the infected areas. These investigators instructed their patients to spray the nose with the vasoconstrictor solution every three or four hours in addition to the penicillin application.
It occurred to us that such medication could be simplified by combining the penicillin with the ephedrine solution, providing the stability of the penicillin is not adversely affected during the period of use.
Since both the sodium and calcium salts of penicillin are available commercially, it seemed desirable to obtain stability information or combinations containing each of these salts. In addition, the stability of crystalline penicillin G1 was also studied * Reccivcd Sept. 4 , 1946, from the Research Division, Presented to the Scientific Section, A. PH. A , . Pittsburgh Cutter Laboratories, Berkeley, Calif. meeting, 1946. 1 Prepared by H. N. Beniams of these laboratories.
๐ SIMILAR VOLUMES
The stability of an oligomeric enzyme, penicillin acylase, was studied in aqueous media. The enzyme was produced by mutant cells of Escherichia coli ATCC 9637, extracted from the periplasmic space by osmotic shock and further puriยฎed using a pseudo-afยฎnity adsorption process. Enzyme stabilisation at