Title : The comparative kinetics of soluble and heparin-Sepharose-immobilized bovine lipoprotein lipase.

Pub. Date : 1983 Oct 1

PMID : 6639055






12 Functional Relationships(s)
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1 The comparative kinetics of soluble and heparin-Sepharose-immobilized bovine lipoprotein lipase. Heparin lipoprotein lipase Bos taurus
2 Hence kinetic parameters of S-LPL and heparin-Sepharose-immobilized LPL (B-LPL) were compared. Heparin lipoprotein lipase Bos taurus
3 Dixon plots of experiments with S-LPL indicated that heparin is a competitive inhibitor against both C-II and TG, and that the binding of either C-II or heparin to the enzyme is a mutually exclusive event. Heparin lipoprotein lipase Bos taurus
4 From the Dixon plots, the dissociation constant Ki for the LPL:heparin binary complex was determined to be 5.0 X 10(-8) M. In contrast to the heparin inhibitory effect on LPL activity against triolein, heparin had no effect on the esterase activity of LPL against p-nitrophenylacetate or p-nitrophenylbutyrate. Heparin lipoprotein lipase Bos taurus
5 From the Dixon plots, the dissociation constant Ki for the LPL:heparin binary complex was determined to be 5.0 X 10(-8) M. In contrast to the heparin inhibitory effect on LPL activity against triolein, heparin had no effect on the esterase activity of LPL against p-nitrophenylacetate or p-nitrophenylbutyrate. Heparin lipoprotein lipase Bos taurus
6 From the Dixon plots, the dissociation constant Ki for the LPL:heparin binary complex was determined to be 5.0 X 10(-8) M. In contrast to the heparin inhibitory effect on LPL activity against triolein, heparin had no effect on the esterase activity of LPL against p-nitrophenylacetate or p-nitrophenylbutyrate. Heparin lipoprotein lipase Bos taurus
7 From the Dixon plots, the dissociation constant Ki for the LPL:heparin binary complex was determined to be 5.0 X 10(-8) M. In contrast to the heparin inhibitory effect on LPL activity against triolein, heparin had no effect on the esterase activity of LPL against p-nitrophenylacetate or p-nitrophenylbutyrate. Heparin lipoprotein lipase Bos taurus
8 From the Dixon plots, the dissociation constant Ki for the LPL:heparin binary complex was determined to be 5.0 X 10(-8) M. In contrast to the heparin inhibitory effect on LPL activity against triolein, heparin had no effect on the esterase activity of LPL against p-nitrophenylacetate or p-nitrophenylbutyrate. Heparin lipoprotein lipase Bos taurus
9 It is concluded that most of the LPL bound to heparin-Sepharose is probably inaccessible to substrate, hence a low Vmax. Heparin lipoprotein lipase Bos taurus
10 However, Km (C-II) and Km (TG) were higher for B-LPL due to the competitive inhibitory effect of heparin on LPL. Heparin lipoprotein lipase Bos taurus
11 However, Km (C-II) and Km (TG) were higher for B-LPL due to the competitive inhibitory effect of heparin on LPL. Heparin lipoprotein lipase Bos taurus
12 Consistent with these kinetic analyses and with the use of human very low density lipoproteins (VLDL) as substrate, S-LPL, even in the presence of heparin, was found to have an apparent rate of lipolysis of VLDL approximately ninefold greater than B-LPL. Heparin lipoprotein lipase Bos taurus