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Chemical Modification of the Porcine Pancreatic Lipase
Lookene, Aivar Sikk, Peeter
Lookene, Aivar
Sikk, Peeter
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Issue Date
1991
Submitted date
2024-03-20
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Abstract
In this low-scope review we summarized the results which typically have not been publishedyet as full papers. To our opinion these data could be valuable for the discussion of the recently published [1] three-dimensional structure of human pancreatic lipase optained by the X-ray crystallography studies. The effect of the modification of several residues in porcine pancreatic lipase has been studied primarily in terms of changes in the steady-state kinetics binding and rate constants which could be determined in the assay system containing lipase (L), variable amounts ofcolipase (C), micellar NaTDC! (bs) and excess of tributyrylglycerol emulsion (S). The approach is based on the assumption that the enzyme does not have anyactivity in the presence of micellar NaTDC and absence ofcolipase due to the displacementof the enzyme from the substrate-water interphase [2, 3], and hasbeen first used by Rathelot etal. [4, 5]. This assumption is correct provided that traces of colipase have been removed from lipase preparations (on a Sephadex LH-60 column [6]). Formally, since the observed dissociation constant of the lipase/colipase interfacial complex, K,””, is typically less, or comparable, with the total enzyme concentration. In conditions K,*? >> [L], Eqn. 2 reduced to a common hyperbolic (Michaelis-type) relationship.
Citation
Lipases : structure, mechanism and genetic engineering, 165 - 172
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Book chapter
conference paper
conference paper
Language
en
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Series/Report no.
GBF monographs ; Volume 16
ISSN
0930-4320
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ISBN
156081165X
3527283323
3527283323
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Attribution-NonCommercial-ShareAlike 4.0 International