Post-heparin phospholipase
Egg phosphatidyl ethanolamine is degraded to lysophosphatidyl ethanolamine and fatty acids by a phospholipase in post-heparin plasma at rates of 10 to 30 μmoles/hr per ml plasma. The optimal system for measuring this enzyme contained albumin and (NH4)2SO4, and the optimal pH was 8.8–9.1. Only slight...
| Main Authors: | , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
Elsevier
1964-04-01
|
| Series: | Journal of Lipid Research |
| Online Access: | http://www.sciencedirect.com/science/article/pii/S0022227520402354 |
| id |
doaj-b6d4dd9a7b0541a7972f76b7c7d889a8 |
|---|---|
| record_format |
Article |
| spelling |
doaj-b6d4dd9a7b0541a7972f76b7c7d889a82021-04-23T06:12:19ZengElsevierJournal of Lipid Research0022-22751964-04-0152177183Post-heparin phospholipaseWilliam C. Vogel0Leslie Zieve1Laboratory for Cancer Research, Radioisotope Service and Department of Medicine, Minneapolis Veterans Hospital, University of Minnesota, Minneapolis, MinnesotaLaboratory for Cancer Research, Radioisotope Service and Department of Medicine, Minneapolis Veterans Hospital, University of Minnesota, Minneapolis, MinnesotaEgg phosphatidyl ethanolamine is degraded to lysophosphatidyl ethanolamine and fatty acids by a phospholipase in post-heparin plasma at rates of 10 to 30 μmoles/hr per ml plasma. The optimal system for measuring this enzyme contained albumin and (NH4)2SO4, and the optimal pH was 8.8–9.1. Only slight degradation of egg or beef lecithin occurred.Post-heparin and pancreatic phospholipase differ in heat stability; in the inhibiting effects of EDTA, HgCl2, and diethyl-p-nitrophenyl phosphate; in the requirement for deoxycholate or albumin; and in an apparent specificity of the post-heparin enzyme for the ethanolamine phosphatide.http://www.sciencedirect.com/science/article/pii/S0022227520402354 |
| collection |
DOAJ |
| language |
English |
| format |
Article |
| sources |
DOAJ |
| author |
William C. Vogel Leslie Zieve |
| spellingShingle |
William C. Vogel Leslie Zieve Post-heparin phospholipase Journal of Lipid Research |
| author_facet |
William C. Vogel Leslie Zieve |
| author_sort |
William C. Vogel |
| title |
Post-heparin phospholipase |
| title_short |
Post-heparin phospholipase |
| title_full |
Post-heparin phospholipase |
| title_fullStr |
Post-heparin phospholipase |
| title_full_unstemmed |
Post-heparin phospholipase |
| title_sort |
post-heparin phospholipase |
| publisher |
Elsevier |
| series |
Journal of Lipid Research |
| issn |
0022-2275 |
| publishDate |
1964-04-01 |
| description |
Egg phosphatidyl ethanolamine is degraded to lysophosphatidyl ethanolamine and fatty acids by a phospholipase in post-heparin plasma at rates of 10 to 30 μmoles/hr per ml plasma. The optimal system for measuring this enzyme contained albumin and (NH4)2SO4, and the optimal pH was 8.8–9.1. Only slight degradation of egg or beef lecithin occurred.Post-heparin and pancreatic phospholipase differ in heat stability; in the inhibiting effects of EDTA, HgCl2, and diethyl-p-nitrophenyl phosphate; in the requirement for deoxycholate or albumin; and in an apparent specificity of the post-heparin enzyme for the ethanolamine phosphatide. |
| url |
http://www.sciencedirect.com/science/article/pii/S0022227520402354 |
| work_keys_str_mv |
AT williamcvogel postheparinphospholipase AT lesliezieve postheparinphospholipase |
| _version_ |
1721513364865155072 |