Bile-Salt-Stimulated Human Milk Lipase: Interaction with Proteins
| Autor: | Bridget M. Sutton, Charmian J. O'Connor, Paul A.G. Butler |
|---|---|
| Rok vydání: | 1988 |
| Předmět: |
Lipoprotein lipase
Chromatography Polymers and Plastics biology Lactoferrin 0206 medical engineering Triacylglycerol lipase Bioengineering 02 engineering and technology 021001 nanoscience & nanotechnology 020601 biomedical engineering Esterase Melittin Biomaterials chemistry.chemical_compound chemistry Biochemistry Materials Chemistry biology.protein Triolein Lysozyme Lipase 0210 nano-technology |
| Zdroj: | Journal of Bioactive and Compatible Polymers. 3:390-402 |
| ISSN: | 1530-8030 0883-9115 |
| DOI: | 10.1177/088391158800300405 |
| Popis: | The initial rates of hydrolysis of triolein, catalyzed by bile-salt-stimulated hu man milk lipase, BSSL, were measured at pH 7.5 and 37 ° C, in the presence of selected proteins, namely immunoglobulin A, α-lactalbumin, lactoferrin, hen egg white lysozyme, pancreatic lipase, myoglobin and the very surface active protein melittin. The esterase activity of the enzyme against 4-nitro- phenylacetate was also measured in the presence of a number of different samples of lactoferrin. Under the conditions used, α-lactalbumin and hen egg white lysozyme had almost no effect on the lipase activity. Immunoglobulin A was slightly inhibitory; lactoferrin, pancreatic lipase and myoglobin were all partially inhibitory; and melittin was capable of almost completely inac tivating the lipase. |
| Databáze: | OpenAIRE |
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