Separation of molecular species of lipoprotein lipase from adipose tissue
When NH4OH–NH4Cl extracts of adipose acetone powder were applied to agarose gel chromatography columns, two peaks of lipoprotein lipase were eluted. The first activity peak (LPLa) was eluted with an elution volume of a protein of molecular weight approximately five times that of the second (LPLb). A...
| الحاوية / القاعدة: | Journal of Lipid Research |
|---|---|
| المؤلفون الرئيسيون: | , |
| التنسيق: | مقال |
| اللغة: | الإنجليزية |
| منشور في: |
Elsevier
1972-01-01
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| الموضوعات: | |
| الوصول للمادة أونلاين: | http://www.sciencedirect.com/science/article/pii/S0022227520394372 |
| _version_ | 1852726431281315840 |
|---|---|
| author | Arlene S. Garfinkel Michael C. Schotz |
| author_facet | Arlene S. Garfinkel Michael C. Schotz |
| author_sort | Arlene S. Garfinkel |
| collection | DOAJ |
| container_title | Journal of Lipid Research |
| description | When NH4OH–NH4Cl extracts of adipose acetone powder were applied to agarose gel chromatography columns, two peaks of lipoprotein lipase were eluted. The first activity peak (LPLa) was eluted with an elution volume of a protein of molecular weight approximately five times that of the second (LPLb). Addition of heparin to the eluted fractions markedly stimulated activity of LPLa, but suppressed that of LPLb. Both lipases had the characteristics that distinguish lipoprotein lipase from other tissue lipases: a requirement for serum for substrate activation, inhibition by 1 m NaCl, and an alkaline pH optimum (pH 8.0). It is concluded that these fractions represent two species of lipoprotein lipase. |
| format | Article |
| id | doaj-art-4dedf8348daf4e77b4fe5a4d0c3d4856 |
| institution | Directory of Open Access Journals |
| issn | 0022-2275 |
| language | English |
| publishDate | 1972-01-01 |
| publisher | Elsevier |
| record_format | Article |
| spelling | doaj-art-4dedf8348daf4e77b4fe5a4d0c3d48562025-08-19T21:10:22ZengElsevierJournal of Lipid Research0022-22751972-01-01131636810.1016/S0022-2275(20)39437-2Separation of molecular species of lipoprotein lipase from adipose tissueArlene S. Garfinkel0Michael C. Schotz1Research, Veterans Administration Hospital (Wadsworth), Los Angeles, California 90073, and; Department of Biological Chemistry, UCLA School of Medicine, Los Angeles, California 90024Research, Veterans Administration Hospital (Wadsworth), Los Angeles, California 90073, and; Department of Biological Chemistry, UCLA School of Medicine, Los Angeles, California 90024When NH4OH–NH4Cl extracts of adipose acetone powder were applied to agarose gel chromatography columns, two peaks of lipoprotein lipase were eluted. The first activity peak (LPLa) was eluted with an elution volume of a protein of molecular weight approximately five times that of the second (LPLb). Addition of heparin to the eluted fractions markedly stimulated activity of LPLa, but suppressed that of LPLb. Both lipases had the characteristics that distinguish lipoprotein lipase from other tissue lipases: a requirement for serum for substrate activation, inhibition by 1 m NaCl, and an alkaline pH optimum (pH 8.0). It is concluded that these fractions represent two species of lipoprotein lipase.http://www.sciencedirect.com/science/article/pii/S0022227520394372gel filtrationheparinserum activation |
| spellingShingle | Arlene S. Garfinkel Michael C. Schotz Separation of molecular species of lipoprotein lipase from adipose tissue gel filtration heparin serum activation |
| title | Separation of molecular species of lipoprotein lipase from adipose tissue |
| title_full | Separation of molecular species of lipoprotein lipase from adipose tissue |
| title_fullStr | Separation of molecular species of lipoprotein lipase from adipose tissue |
| title_full_unstemmed | Separation of molecular species of lipoprotein lipase from adipose tissue |
| title_short | Separation of molecular species of lipoprotein lipase from adipose tissue |
| title_sort | separation of molecular species of lipoprotein lipase from adipose tissue |
| topic | gel filtration heparin serum activation |
| url | http://www.sciencedirect.com/science/article/pii/S0022227520394372 |
| work_keys_str_mv | AT arlenesgarfinkel separationofmolecularspeciesoflipoproteinlipasefromadiposetissue AT michaelcschotz separationofmolecularspeciesoflipoproteinlipasefromadiposetissue |