Manometric determination of carboxypeptidase
โ Scribed by Charles A. Zittle
- Publisher
- Elsevier Science
- Year
- 1948
- Tongue
- English
- Weight
- 131 KB
- Volume
- 246
- Category
- Article
- ISSN
- 0016-0032
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โฆ Synopsis
Manometric Determination of Carboxypeptidase.--CHARLES A. ZITTLE. Carboxypeptidase has been estimated by formol titration with chloracetyltyrosine as the substrate (1). This enzyme retains much of its activity in the presence of formaldehyde and in the procedure mentioned formaldehyde is added at the beginning of the estimation. The amino group of the tyrosine released by hydrolysis is masked by the formaldehyde and the strong monochloracetic acid is readily measured. In the above procedure the acid is estimated by titration at the end of the experiment. This acid also could be conveniently measured manometrically with NaHCO3 present, which would offer the advantage that the acid release could be followed throughout the experiment. The utilization of the manometric procedure is described herein.
EXPERIMENTAL.
๐ SIMILAR VOLUMES
A method is described for manometric determination of bicarbonate (as little as 0.25 pmoles) in leaves. Conditions such as optimum pH and inactivation of carbonic anhydrase are introduced to stabilize the bicarbonate. Crude leaf extracts are purified with chloroform and Darco G-60. An ionic mixture