How gastric lipase, an interfacial enzyme with a Ser-His-Asp catalytic triad, acts optimally at acidic pH.
about
Self-renewal of the human gastric epithelium: new insights from expression profiling using laser microdissection.Role of the gut in modulating lipoprotein metabolism.The metabolic serine hydrolases and their functions in mammalian physiology and disease.Effects of surfactants on lipase structure, activity, and inhibition.A survey of the 2006-2009 quartz crystal microbalance biosensor literature.Relevant pH and lipase for in vitro models of gastric digestion.In vitro digestion of the self-emulsifying lipid excipient Labrasol(®) by gastrointestinal lipases and influence of its colloidal structure on lipolysis rate.pH effects on the structural dynamics of cutinase from Trichoderma reesei: insights from molecular dynamics simulations.
P2860
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P2860
How gastric lipase, an interfacial enzyme with a Ser-His-Asp catalytic triad, acts optimally at acidic pH.
description
2006 nî lūn-bûn
@nan
2006年の論文
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2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
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2006年论文
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2006年论文
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name
How gastric lipase, an interfa ...... , acts optimally at acidic pH.
@en
How gastric lipase, an interfa ...... , acts optimally at acidic pH.
@nl
type
label
How gastric lipase, an interfa ...... , acts optimally at acidic pH.
@en
How gastric lipase, an interfa ...... , acts optimally at acidic pH.
@nl
prefLabel
How gastric lipase, an interfa ...... , acts optimally at acidic pH.
@en
How gastric lipase, an interfa ...... , acts optimally at acidic pH.
@nl
P2093
P356
P1433
P1476
How gastric lipase, an interfa ...... d, acts optimally at acidic pH
@en
P2093
Coralie Attias
Henri Chahinian
Peter Fojan
Torben Snabe
P304
P356
10.1021/BI0518803
P407
P577
2006-01-01T00:00:00Z