Reaffirmation of the validity of enzymatic cleavage of lithocholic acid from N-epsilon-lithocholyl-L-lysine and N-alpha-CBZ-N-epsilon-lithocholyl-L-lysine.
N-epsilon-lithocholyl-L-lysine or N-alpha-CBZ-N-epsilon-lithocholyl-L-lysine when incubated overnight at 37 degrees C with 3 K units of clostridial cholanoylaminoacid hydrolase (from Clostridium perfringens ATCC 19574) in the presence of disodium EDTA (0.1 M), beta-mercaptoethanol (0.1 M), and sodiu...
| Main Authors: | , , |
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| Format: | Article |
| Language: | English |
| Published: |
Elsevier
1988-10-01
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| Series: | Journal of Lipid Research |
| Online Access: | http://www.sciencedirect.com/science/article/pii/S0022227520387794 |
| _version_ | 1818727189676294144 |
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| author | P P Nair G Kessie V P Flanagan |
| author_facet | P P Nair G Kessie V P Flanagan |
| author_sort | P P Nair |
| collection | DOAJ |
| description | N-epsilon-lithocholyl-L-lysine or N-alpha-CBZ-N-epsilon-lithocholyl-L-lysine when incubated overnight at 37 degrees C with 3 K units of clostridial cholanoylaminoacid hydrolase (from Clostridium perfringens ATCC 19574) in the presence of disodium EDTA (0.1 M), beta-mercaptoethanol (0.1 M), and sodium acetate buffer, pH 5.6, released free lithocholic acid. The latter material was isolated by thin-layer chromatography and identified by combined gas-liquid chromatography-mass spectrometry in the full scan and selected-ion mode. In order to maintain its activity, the enzyme was always stored in 1.0-ml aliquots at temperatures below -20 degrees C and each aliquot when thawed was used immediately; any left over enzyme was never reused. Contrary to the observations of Yanagisawa et al. (J. Lipid Res. 1984. 25: 1263-1271) the results of this study reaffirm the validity of the original observations on the enzymatic cleavage of lithocholic acid from tissue-bound form. |
| first_indexed | 2024-12-17T22:10:09Z |
| format | Article |
| id | doaj.art-1422757f0f3c482db449c13c65df7b59 |
| institution | Directory Open Access Journal |
| issn | 0022-2275 |
| language | English |
| last_indexed | 2024-12-17T22:10:09Z |
| publishDate | 1988-10-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Journal of Lipid Research |
| spelling | doaj.art-1422757f0f3c482db449c13c65df7b592022-12-21T21:30:46ZengElsevierJournal of Lipid Research0022-22751988-10-01278905909Reaffirmation of the validity of enzymatic cleavage of lithocholic acid from N-epsilon-lithocholyl-L-lysine and N-alpha-CBZ-N-epsilon-lithocholyl-L-lysine.P P NairG KessieV P FlanaganN-epsilon-lithocholyl-L-lysine or N-alpha-CBZ-N-epsilon-lithocholyl-L-lysine when incubated overnight at 37 degrees C with 3 K units of clostridial cholanoylaminoacid hydrolase (from Clostridium perfringens ATCC 19574) in the presence of disodium EDTA (0.1 M), beta-mercaptoethanol (0.1 M), and sodium acetate buffer, pH 5.6, released free lithocholic acid. The latter material was isolated by thin-layer chromatography and identified by combined gas-liquid chromatography-mass spectrometry in the full scan and selected-ion mode. In order to maintain its activity, the enzyme was always stored in 1.0-ml aliquots at temperatures below -20 degrees C and each aliquot when thawed was used immediately; any left over enzyme was never reused. Contrary to the observations of Yanagisawa et al. (J. Lipid Res. 1984. 25: 1263-1271) the results of this study reaffirm the validity of the original observations on the enzymatic cleavage of lithocholic acid from tissue-bound form.http://www.sciencedirect.com/science/article/pii/S0022227520387794 |
| spellingShingle | P P Nair G Kessie V P Flanagan Reaffirmation of the validity of enzymatic cleavage of lithocholic acid from N-epsilon-lithocholyl-L-lysine and N-alpha-CBZ-N-epsilon-lithocholyl-L-lysine. Journal of Lipid Research |
| title | Reaffirmation of the validity of enzymatic cleavage of lithocholic acid from N-epsilon-lithocholyl-L-lysine and N-alpha-CBZ-N-epsilon-lithocholyl-L-lysine. |
| title_full | Reaffirmation of the validity of enzymatic cleavage of lithocholic acid from N-epsilon-lithocholyl-L-lysine and N-alpha-CBZ-N-epsilon-lithocholyl-L-lysine. |
| title_fullStr | Reaffirmation of the validity of enzymatic cleavage of lithocholic acid from N-epsilon-lithocholyl-L-lysine and N-alpha-CBZ-N-epsilon-lithocholyl-L-lysine. |
| title_full_unstemmed | Reaffirmation of the validity of enzymatic cleavage of lithocholic acid from N-epsilon-lithocholyl-L-lysine and N-alpha-CBZ-N-epsilon-lithocholyl-L-lysine. |
| title_short | Reaffirmation of the validity of enzymatic cleavage of lithocholic acid from N-epsilon-lithocholyl-L-lysine and N-alpha-CBZ-N-epsilon-lithocholyl-L-lysine. |
| title_sort | reaffirmation of the validity of enzymatic cleavage of lithocholic acid from n epsilon lithocholyl l lysine and n alpha cbz n epsilon lithocholyl l lysine |
| url | http://www.sciencedirect.com/science/article/pii/S0022227520387794 |
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