Purification of pancreatic lipase via its affinity for bile salts and apolar surfaces.
An improved method for the purification of pancreatic lipase in milligram amounts is described. Only one batch step and one chromatographic step are required to produce a lipase-colipase complex and a lipase largely free of colipase. Both species are lipid free; physical and kinetic data indicate th...
| Main Authors: | , |
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| Format: | Article |
| Language: | English |
| Published: |
Elsevier
1978-11-01
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| Series: | Journal of Lipid Research |
| Online Access: | http://www.sciencedirect.com/science/article/pii/S002222752040687X |
| _version_ | 1819076430704672768 |
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| author | W E Momsen H L Brockman |
| author_facet | W E Momsen H L Brockman |
| author_sort | W E Momsen |
| collection | DOAJ |
| description | An improved method for the purification of pancreatic lipase in milligram amounts is described. Only one batch step and one chromatographic step are required to produce a lipase-colipase complex and a lipase largely free of colipase. Both species are lipid free; physical and kinetic data indicate that the predominant lipase species is lipase B. |
| first_indexed | 2024-12-21T18:41:11Z |
| format | Article |
| id | doaj.art-b0c8bc33d2cb4fd4b7cb48e5e20f10bc |
| institution | Directory Open Access Journal |
| issn | 0022-2275 |
| language | English |
| last_indexed | 2024-12-21T18:41:11Z |
| publishDate | 1978-11-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Journal of Lipid Research |
| spelling | doaj.art-b0c8bc33d2cb4fd4b7cb48e5e20f10bc2022-12-21T18:54:00ZengElsevierJournal of Lipid Research0022-22751978-11-0119810321037Purification of pancreatic lipase via its affinity for bile salts and apolar surfaces.W E MomsenH L BrockmanAn improved method for the purification of pancreatic lipase in milligram amounts is described. Only one batch step and one chromatographic step are required to produce a lipase-colipase complex and a lipase largely free of colipase. Both species are lipid free; physical and kinetic data indicate that the predominant lipase species is lipase B.http://www.sciencedirect.com/science/article/pii/S002222752040687X |
| spellingShingle | W E Momsen H L Brockman Purification of pancreatic lipase via its affinity for bile salts and apolar surfaces. Journal of Lipid Research |
| title | Purification of pancreatic lipase via its affinity for bile salts and apolar surfaces. |
| title_full | Purification of pancreatic lipase via its affinity for bile salts and apolar surfaces. |
| title_fullStr | Purification of pancreatic lipase via its affinity for bile salts and apolar surfaces. |
| title_full_unstemmed | Purification of pancreatic lipase via its affinity for bile salts and apolar surfaces. |
| title_short | Purification of pancreatic lipase via its affinity for bile salts and apolar surfaces. |
| title_sort | purification of pancreatic lipase via its affinity for bile salts and apolar surfaces |
| url | http://www.sciencedirect.com/science/article/pii/S002222752040687X |
| work_keys_str_mv | AT wemomsen purificationofpancreaticlipaseviaitsaffinityforbilesaltsandapolarsurfaces AT hlbrockman purificationofpancreaticlipaseviaitsaffinityforbilesaltsandapolarsurfaces |