The carboxypeptidase activity of pancreatin U. S. P
β Scribed by Bauer, Charles W. ;Miskinis, Alphonse M.
- Publisher
- Elsevier
- Year
- 1947
- Weight
- 410 KB
- Volume
- 36
- Category
- Article
- ISSN
- 0095-9553
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β¦ Synopsis
by digestion upon a specially prepared solution of casein.
A modification of both the U. S. P. and the Willson methods has been made in the preparation of the casein solution.
- Samples of commercial trypsin were also assayed by the modified Willson method, and the results have been compared with U. S. Pharmacopeia Reference Trypsin.
It has been demonstrated by these assays that "Triple Strength!' Pancreatin possesses three times the potency of the minimum requirements as stated in the official monograph; but, that it is misleading to imply that it posesses three times the potency of Pancreatin U. S. P.
REFERENCES
(1) Kiihne, W., quoted from Oppenheimer, C., "Die Permente und ihre Wirkungen," Leipzig, 1926, ed. 5, vol. 2, p. 894. 5 WNlllson F. E Tma JOURNAL, 19, 12&29(1930). (2) Purkinje and Pappenheim (1836). quoted from Oppenheimer C. ibid sup. p. 894. du Carlsberg 7 (1907) (3). Corbisakt, L."R. F.' E., quoted from Oppenheimer. C., OP. cat., p. 894.
π SIMILAR VOLUMES
## Abstract Carboxypeptidase G2 (CPG2) is a bacterial enzyme that is currently employed in a range of targeted cancer chemotherapy strategies such as geneβdirected enzyme prodrug therapy (GDEPT). Employing dynamic nuclear polarization (DNP) and natural abundance ^13^C magnetic resonance spectroscop