Further studies on bacterial and liver tryptophan pyrrolases
| ISSN: |
0005-2744
|
|---|---|
| Source: |
Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
|
| Topics: |
Biology
|
| Type of Medium: |
Electronic Resource
|
| URL: |
| _version_ | 1798292369722834944 |
|---|---|
| autor | Tokuyama, K. |
| autorsonst | Tokuyama, K. |
| book_url | http://linkinghub.elsevier.com/retrieve/pii/0005-2744(68)90163-0 |
| datenlieferant | nat_lic_papers |
| fussnote | Tryptophan pyrrolase was isolated and extensively purified from rat liver and Pseudomonas sp. (ATCC 14675) and the properties of the two preparations were compared. They possess in common the following characteristics: (1) Requirement for a reducing agent to start reaction, (2) Appearance of a lag period in reaction kinetics following preincubation with reducing agent. (3) pH optima in the range 5.5-8.0 (8.0 and 7.0-7.4 for bacterial and liver enzyme respectively). (4) Inhibition by SH reagents and heme- or hematin-chelating reagents added during reaction. (5) Spectral changes in the Soret region during reaction. (6) A mol.wt. of 103 000 measured in sucrose gradients.The bacterial enzyme is more stable under a variety of conditions than is the liver enzyme; it contains hematin in a more tightly bound form than liver enzyme.The nature of the prosthetic group and the protein conformation in the active form of the enzyme are discussed. |
| hauptsatz | hsatz_simple |
| identnr | NLZ185754910 |
| issn | 0005-2744 |
| journal_name | BBA - Enzymology |
| materialart | 1 |
| package_name | Elsevier |
| publikationsort | Amsterdam |
| publisher | Elsevier |
| reference | 151 (1968), S. 76-87 |
| search_space | articles |
| shingle_author_1 | Tokuyama, K. |
| shingle_author_2 | Tokuyama, K. |
| shingle_author_3 | Tokuyama, K. |
| shingle_author_4 | Tokuyama, K. |
| shingle_catch_all_1 | Tokuyama, K. Further studies on bacterial and liver tryptophan pyrrolases 0005-2744 00052744 Elsevier |
| shingle_catch_all_2 | Tokuyama, K. Further studies on bacterial and liver tryptophan pyrrolases 0005-2744 00052744 Elsevier |
| shingle_catch_all_3 | Tokuyama, K. Further studies on bacterial and liver tryptophan pyrrolases 0005-2744 00052744 Elsevier |
| shingle_catch_all_4 | Tokuyama, K. Further studies on bacterial and liver tryptophan pyrrolases 0005-2744 00052744 Elsevier |
| shingle_title_1 | Further studies on bacterial and liver tryptophan pyrrolases |
| shingle_title_2 | Further studies on bacterial and liver tryptophan pyrrolases |
| shingle_title_3 | Further studies on bacterial and liver tryptophan pyrrolases |
| shingle_title_4 | Further studies on bacterial and liver tryptophan pyrrolases |
| sigel_instance_filter | dkfz geomar wilbert ipn albert fhp |
| source_archive | Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 |
| timestamp | 2024-05-06T08:47:25.843Z |
| titel | Further studies on bacterial and liver tryptophan pyrrolases |
| titel_suche | Further studies on bacterial and liver tryptophan pyrrolases Tryptophan pyrrolase was isolated and extensively purified from rat liver and Pseudomonas sp. (ATCC 14675) and the properties of the two preparations were compared. They possess in common the following characteristics: (1) Requirement for a reducing agent to start reaction, (2) Appearance of a lag period in reaction kinetics following preincubation with reducing agent. (3) pH optima in the range 5.5-8.0 (8.0 and 7.0-7.4 for bacterial and liver enzyme respectively). (4) Inhibition by SH reagents and heme- or hematin-chelating reagents added during reaction. (5) Spectral changes in the Soret region during reaction. (6) A mol.wt. of 103 000 measured in sucrose gradients.The bacterial enzyme is more stable under a variety of conditions than is the liver enzyme; it contains hematin in a more tightly bound form than liver enzyme.The nature of the prosthetic group and the protein conformation in the active form of the enzyme are discussed. |
| topic | W |
| uid | nat_lic_papers_NLZ185754910 |