Characterization of phospholipase B of Culex pipiens fatigans

Phospholipase B has been found in the mosquito Culex pipiens fatigans, and some of its properties have been studied. The enzyme had a high optimum temperature (45°C) and broad alkaline pH optimum (8-9). It was inactive toward diacylphospholipids, and hydrolyzed lysolecithin at a higher rate than lys...

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Main Authors: R. Hanumantha Rao, D. Subrahmanyam
Format: Article
Language:English
Published: Elsevier 1969-11-01
Series:Journal of Lipid Research
Subjects:
Online Access:http://www.sciencedirect.com/science/article/pii/S0022227520430238
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author R. Hanumantha Rao
D. Subrahmanyam
author_facet R. Hanumantha Rao
D. Subrahmanyam
author_sort R. Hanumantha Rao
collection DOAJ
description Phospholipase B has been found in the mosquito Culex pipiens fatigans, and some of its properties have been studied. The enzyme had a high optimum temperature (45°C) and broad alkaline pH optimum (8-9). It was inactive toward diacylphospholipids, and hydrolyzed lysolecithin at a higher rate than lysophosphatidyl ethanolamine. The enzyme was heat labile, but lysolecithin protected it against heat inactivation. Phosphatidyl ethanolamine, phosphatidyl choline, deoxycholate, Fe+++, and Hg++ inhibited the enzyme markedly.The enzyme was present mainly in larvae; little enzyme activity was detected in pupae or adults. The total and specific activities were highest in IV instar (6 day) and I instar (1st day) larvae, respectively. It was localized in the microsomal fraction and was distributed mainly in the abdomen and thorax of the insect. The enzyme was present at much higher levels of activity in larvae of the mosquitoes Anopheles stephensi and Aedes aegypti.
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spelling doaj.art-f974cb8b5c9b492db108c03eae1ee02f2022-12-21T19:03:02ZengElsevierJournal of Lipid Research0022-22751969-11-01106636641Characterization of phospholipase B of Culex pipiens fatigansR. Hanumantha Rao0D. Subrahmanyam1Biochemistry Division, National Institute of Communicable Diseases, Delhi, IndiaBiochemistry Division, National Institute of Communicable Diseases, Delhi, IndiaPhospholipase B has been found in the mosquito Culex pipiens fatigans, and some of its properties have been studied. The enzyme had a high optimum temperature (45°C) and broad alkaline pH optimum (8-9). It was inactive toward diacylphospholipids, and hydrolyzed lysolecithin at a higher rate than lysophosphatidyl ethanolamine. The enzyme was heat labile, but lysolecithin protected it against heat inactivation. Phosphatidyl ethanolamine, phosphatidyl choline, deoxycholate, Fe+++, and Hg++ inhibited the enzyme markedly.The enzyme was present mainly in larvae; little enzyme activity was detected in pupae or adults. The total and specific activities were highest in IV instar (6 day) and I instar (1st day) larvae, respectively. It was localized in the microsomal fraction and was distributed mainly in the abdomen and thorax of the insect. The enzyme was present at much higher levels of activity in larvae of the mosquitoes Anopheles stephensi and Aedes aegypti.http://www.sciencedirect.com/science/article/pii/S0022227520430238mosquito vectorsdevelopmental stageslysophospholipidsalkaline pH optimumhigh optimum temperaturedeoxycholate
spellingShingle R. Hanumantha Rao
D. Subrahmanyam
Characterization of phospholipase B of Culex pipiens fatigans
Journal of Lipid Research
mosquito vectors
developmental stages
lysophospholipids
alkaline pH optimum
high optimum temperature
deoxycholate
title Characterization of phospholipase B of Culex pipiens fatigans
title_full Characterization of phospholipase B of Culex pipiens fatigans
title_fullStr Characterization of phospholipase B of Culex pipiens fatigans
title_full_unstemmed Characterization of phospholipase B of Culex pipiens fatigans
title_short Characterization of phospholipase B of Culex pipiens fatigans
title_sort characterization of phospholipase b of culex pipiens fatigans
topic mosquito vectors
developmental stages
lysophospholipids
alkaline pH optimum
high optimum temperature
deoxycholate
url http://www.sciencedirect.com/science/article/pii/S0022227520430238
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