| Autor: |
Hans Otto Hansen, Leif Rasmussen, J. Florin-Christensen, M. Florin-Christensen, Jens Knudsen |
| Rok vydání: |
1986 |
| Předmět: |
|
| Zdroj: |
Comparative Biochemistry and Physiology Part B: Comparative Biochemistry. 85:149-155 |
| ISSN: |
0305-0491 |
| DOI: |
10.1016/0305-0491(86)90237-3 |
| Popis: |
1. 1. A phospholipase A and a triacylglycerol lipase from Tetrahymena thermophila culture medium were isolated and characterized. 2. 2. Phospholipase A, which was shown to be of type A1 (EC. 3.1.1.32) was purified 547-fold. It hydrolyzed 1-palmitoyl-2-[1-14C]oleoyl-sn-glycerol-3-phosphorylcholine with a pH optimum of 4.5 and did not require Ca2+ ions for its activity. Its estimated mol.wt determined by gel filtration on Sephadex G 75 was 28,000 daltons. 3. 3. Triacylglycerol lipase (EC. 3.1.1.3), a hitherto unobserved activity from Tetrahymena medium, was purified 818-fold. It hydrolyzed tri[1-14C]oleoylglycerol, mainly in position sn-1 with a pH optimum of 4.4. The enzyme was also active on diacylglycerol. The activity was not affected by addition of Ca2+ ions or EDTA. It eluted from Sephadex G75 with an estimated mol.wt of 30,500 daltons. 4. 4. The origin and significance of these enzymes as well as possible adaptations of the cells to their presence in the medium are discussed. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
|
