Effect of an anti-lipoprotein lipase serum on plasma triglyceride removal
Anti-lipoprotein lipase sera injected intravenously in roosters blocked quantitatively the catabolism of very low density lipoprotein (VLDL) triglyceride. Antibodies were produced in rabbits immunized with highly purified lipoprotein lipase (LPL, glycerol ester hydrolase, E C 3.1.1.3) prepared from...
| Main Authors: | , , |
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| Format: | Article |
| Language: | English |
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Elsevier
1976-09-01
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| Series: | Journal of Lipid Research |
| Subjects: | |
| Online Access: | http://www.sciencedirect.com/science/article/pii/S0022227520417481 |
| _version_ | 1818743072446480384 |
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| author | I P Kompiang Dr A Bensadoun M W Yang |
| author_facet | I P Kompiang Dr A Bensadoun M W Yang |
| author_sort | I P Kompiang |
| collection | DOAJ |
| description | Anti-lipoprotein lipase sera injected intravenously in roosters blocked quantitatively the catabolism of very low density lipoprotein (VLDL) triglyceride. Antibodies were produced in rabbits immunized with highly purified lipoprotein lipase (LPL, glycerol ester hydrolase, E C 3.1.1.3) prepared from chicken adipose tissue. Following anti-LPL serum injection there was a linear increase in plasma triglyceride concentration. The rate of entry of triglyceride in plasma was estimated from the rate of triglyceride accumulation in the plasma of animals injected with anti-LPL serum, or from the disappearance curve of biologically labelled VLDL. In instances where both measurements were conducted in the same animals there was very close agreement between the two procedures. Inhibition of VLDL triglyceride catabolism of anti-LPL serum provided a way to characterize newly secreted VLDL that exhibited a broad spectrum of particle sizes with a median of 625 Å. They contained 76.2 ± 1.2% triglyceride and had a high ratio of free to ester cholesterol (2.46 ± 0.45). In control VLDL samples there was 46.1% triglyceride, and the ratio of free to ester cholesterol was 1.19. The complete inhibition of triglyceride removal by an antiserum prepared against adipose tissue LPL demonstrates that the NaCl-inhibited, serum-activated lipase prepared by affinity chromatography on heparin-Sepharose and concanavalin A–Sepharose columns is the enzyme responsible in vivo for the catabolism of VLDL triglyceride. Further, the kinetics of triglyceride accumulation in the plasma provide evidence that the site of degradation of VLDL triglyceride is within the plasma compartment. |
| first_indexed | 2024-12-18T02:22:36Z |
| format | Article |
| id | doaj.art-a086b58900da487bab76c4751efef742 |
| institution | Directory Open Access Journal |
| issn | 0022-2275 |
| language | English |
| last_indexed | 2024-12-18T02:22:36Z |
| publishDate | 1976-09-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Journal of Lipid Research |
| spelling | doaj.art-a086b58900da487bab76c4751efef7422022-12-21T21:24:07ZengElsevierJournal of Lipid Research0022-22751976-09-01175498505Effect of an anti-lipoprotein lipase serum on plasma triglyceride removalI P Kompiang0Dr A Bensadoun1M W Yang2Division of Nutritional Sciences, Cornell University, Ithaca, New York 14853Division of Nutritional Sciences, Cornell University, Ithaca, New York 14853; N220 Martha Van Rensselaer Hall, Cornell University, Division of Nutritional Sciences, Ithaca, New York 14853; Address correspondence and reprint requests to Dr. Andre BensadounDivision of Nutritional Sciences, Cornell University, Ithaca, New York 14853Anti-lipoprotein lipase sera injected intravenously in roosters blocked quantitatively the catabolism of very low density lipoprotein (VLDL) triglyceride. Antibodies were produced in rabbits immunized with highly purified lipoprotein lipase (LPL, glycerol ester hydrolase, E C 3.1.1.3) prepared from chicken adipose tissue. Following anti-LPL serum injection there was a linear increase in plasma triglyceride concentration. The rate of entry of triglyceride in plasma was estimated from the rate of triglyceride accumulation in the plasma of animals injected with anti-LPL serum, or from the disappearance curve of biologically labelled VLDL. In instances where both measurements were conducted in the same animals there was very close agreement between the two procedures. Inhibition of VLDL triglyceride catabolism of anti-LPL serum provided a way to characterize newly secreted VLDL that exhibited a broad spectrum of particle sizes with a median of 625 Å. They contained 76.2 ± 1.2% triglyceride and had a high ratio of free to ester cholesterol (2.46 ± 0.45). In control VLDL samples there was 46.1% triglyceride, and the ratio of free to ester cholesterol was 1.19. The complete inhibition of triglyceride removal by an antiserum prepared against adipose tissue LPL demonstrates that the NaCl-inhibited, serum-activated lipase prepared by affinity chromatography on heparin-Sepharose and concanavalin A–Sepharose columns is the enzyme responsible in vivo for the catabolism of VLDL triglyceride. Further, the kinetics of triglyceride accumulation in the plasma provide evidence that the site of degradation of VLDL triglyceride is within the plasma compartment.http://www.sciencedirect.com/science/article/pii/S0022227520417481Lipoprotein lipase antiserumvery low density lipoprotein |
| spellingShingle | I P Kompiang Dr A Bensadoun M W Yang Effect of an anti-lipoprotein lipase serum on plasma triglyceride removal Journal of Lipid Research Lipoprotein lipase antiserum very low density lipoprotein |
| title | Effect of an anti-lipoprotein lipase serum on plasma triglyceride removal |
| title_full | Effect of an anti-lipoprotein lipase serum on plasma triglyceride removal |
| title_fullStr | Effect of an anti-lipoprotein lipase serum on plasma triglyceride removal |
| title_full_unstemmed | Effect of an anti-lipoprotein lipase serum on plasma triglyceride removal |
| title_short | Effect of an anti-lipoprotein lipase serum on plasma triglyceride removal |
| title_sort | effect of an anti lipoprotein lipase serum on plasma triglyceride removal |
| topic | Lipoprotein lipase antiserum very low density lipoprotein |
| url | http://www.sciencedirect.com/science/article/pii/S0022227520417481 |
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