Purification of rat pancreatic lipase
A procedure for the isolation of lipase (glycerolester hydrolase, EC 3.1.1.3) from rat pancreas is described. The purification scheme includes homogenization of the pancreas. centrifugation at 3,000 rpm, centrifugation at 40,000 rpm. DEAE-cellulose chromatography, precipitation of amylase as the amy...
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| Format: | Article |
| Language: | English |
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Elsevier
1968-11-01
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| Series: | Journal of Lipid Research |
| Subjects: | |
| Online Access: | http://www.sciencedirect.com/science/article/pii/S0022227520426951 |
| _version_ | 1830486292529414144 |
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| author | Lewis I. Gidez |
| author_facet | Lewis I. Gidez |
| author_sort | Lewis I. Gidez |
| collection | DOAJ |
| description | A procedure for the isolation of lipase (glycerolester hydrolase, EC 3.1.1.3) from rat pancreas is described. The purification scheme includes homogenization of the pancreas. centrifugation at 3,000 rpm, centrifugation at 40,000 rpm. DEAE-cellulose chromatography, precipitation of amylase as the amylase-glycogen complex, gel filtration of the amylase-free proteins on Sephadex G-100, and chromatography on carboxymethyl-Sephadex C-50. The enzyme showed only one band on polyacrylamide gel electrophoresis and had a specific activity of 5330 ± 80 units/mg of protein. |
| first_indexed | 2024-12-21T18:40:32Z |
| format | Article |
| id | doaj.art-3475c8517b1f4fab84a8e3aadf756b62 |
| institution | Directory Open Access Journal |
| issn | 0022-2275 |
| language | English |
| last_indexed | 2024-12-21T18:40:32Z |
| publishDate | 1968-11-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Journal of Lipid Research |
| spelling | doaj.art-3475c8517b1f4fab84a8e3aadf756b622022-12-21T18:54:01ZengElsevierJournal of Lipid Research0022-22751968-11-0196794798Purification of rat pancreatic lipaseLewis I. Gidez0Institut de Chimie Biologique, Facult; des Sciences, Marseille, France; Departments of Biochemistry and Medicine, Albert Einstein College of Medicine, Yeshiva University, Bronx, New York 10461A procedure for the isolation of lipase (glycerolester hydrolase, EC 3.1.1.3) from rat pancreas is described. The purification scheme includes homogenization of the pancreas. centrifugation at 3,000 rpm, centrifugation at 40,000 rpm. DEAE-cellulose chromatography, precipitation of amylase as the amylase-glycogen complex, gel filtration of the amylase-free proteins on Sephadex G-100, and chromatography on carboxymethyl-Sephadex C-50. The enzyme showed only one band on polyacrylamide gel electrophoresis and had a specific activity of 5330 ± 80 units/mg of protein.http://www.sciencedirect.com/science/article/pii/S0022227520426951amylaseDEAE-celluloseSephadex G-100CM-Sephadex C-50 |
| spellingShingle | Lewis I. Gidez Purification of rat pancreatic lipase Journal of Lipid Research amylase DEAE-cellulose Sephadex G-100 CM-Sephadex C-50 |
| title | Purification of rat pancreatic lipase |
| title_full | Purification of rat pancreatic lipase |
| title_fullStr | Purification of rat pancreatic lipase |
| title_full_unstemmed | Purification of rat pancreatic lipase |
| title_short | Purification of rat pancreatic lipase |
| title_sort | purification of rat pancreatic lipase |
| topic | amylase DEAE-cellulose Sephadex G-100 CM-Sephadex C-50 |
| url | http://www.sciencedirect.com/science/article/pii/S0022227520426951 |
| work_keys_str_mv | AT lewisigidez purificationofratpancreaticlipase |