Phospholipid deacylating activities in murine leprosy bacilli
s.l; s.n; dec. 1980. 8 p. tab, graf.
Non-conventional
de En
| SES-SP, HANSEN, HANSENIASE, SESSP-ILSLACERVO, SES-SP
| ID: biblio-1240713
Bibliothèque responsable:
BR191.1
Localisation: [{"text": "BR191.1", "_a": "00689/s"}]
ABSTRACT
1) The particulate fraction of cultivated murine leprosy bacilli (Mycobacterium lepraemurium, rough colonies of the Hawaiian-Ogawa strain) contained phospholipid deacylating activities with acidic pH optima. It hydrolyzed phosphatidylcholine and phosphatidylethanolamine at similar rates, and phosphatidylinositol oligomannosides more slowly. It also hydrolyzed 1-acyl- and 2-acyl-GPCs (sn-glycerol 3-phosphocholine) more rapidly than phosphatidylcholine. 2) Ca2+ did not stimulate either diacyl- or monoacyl-hydrolase activity. Triton X-100 and Emulgen 913 had little influence on the hydrolysis of phosphatidylcholine, but at rather high concentrations inhibited the hydrolyses of 1-acyl- and 2-acyl-GPCs. Iron ions strongly inhibited the hydrolysis of phosphatidylcholine, but caused little or no inhibition of the deacylations of 1-acyl- and 2-acyl-GPCs. 3) With 1-[stearoyl-14C]phosphatidylcholine and 2-[oleoyl-14C]phosphatidylcholine as substrates, both labeled fatty acid and lysophosphatidylcholine were produced. Labeled fatty acid appeared more rapidly from 2-[oleoyl-14C]phosphatidylcholine than labeled lysophosphatidylcholine, while labeled lysophosphatidylcholine was produced more than labeled fatty acid from 1-[stearoyl-14C]phosphatidylcholine in the early stage of incubation.
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Collection:
06-national
/
BR
Base de données:
HANSEN
/
HANSENIASE
/
SES-SP
/
SESSP-ILSLACERVO
Sujet principal:
Phosphatidylcholines
/
Phospholipides
/
Détergents
/
Température élevée
/
Concentration en ions d'hydrogène
/
Hydrolases
/
Hydrolyse
/
Fer
/
Mycobacterium lepraemurium
Limites:
Animals
Langue:
En
Année:
1980
Type de document:
Non-conventional