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1 rols, exist independently of the presence of colipase.
2 to the putative PTL binding domains of human colipase.
3 es smaller than the area occupied by a bound colipase.
4 o tributyrin to the same extent as wild type colipase.
5 monolayers and emulsions and for binding to colipase.
6 s to change the interaction between hPTL and colipase.
7 5-fold less activity compared with wild-type colipase.
8 to the monolayer of the amphipathic protein, colipase.
9 novel structure involving fatty acid and/or colipase.
10 nction of pancreatic triglyceride lipase and colipase.
11 but shows little additional interaction with colipase.
12 ce, even if procolipase is added before [14C]colipase.
16 is further developed and applied to analyze colipase adsorption rates to mixed monolayers of phospho
19 It is successfully applied to rate data for colipase adsorption to phospholipid alone and yields rea
21 interface or both, influence the binding of colipase and hPTL through interactions with the beta5'-l
22 ray crystal structure of the complex between colipase and lipase suggest another function for colipas
23 function of the interaction between Glu15 of colipase and lipase, we examined one mutant, E15R, in de
25 e may regulate the type of surfaces to which colipase and, hence, lipase bind and may control the spe
26 ase and trypsin, and mRNAs for chymotrypsin, colipase, and others that may derive from uninfected epi
27 human pancreatic triglyceride lipase and of colipase, another pancreatic protein that interacts with
29 his hypothesis by introducing mutations into colipase at position 15, a residue that contacts the lid
32 in proportion to their activity, each mutant colipase bound to tributyrin to the same extent as wild
33 yer differs from the interaction of the hPTL-colipase complex with a dicaprin monolayer or a triglyce
35 These results support the hypothesis that colipase concentrates fatty acids laterally at its perip
37 er of either or both lipids is present, [14C]colipase dominates the adsorption process, even if bile
38 the fatty acid-rich nano-domain surrounding colipase facilitates lipase adsorption in the 'flap-open
43 n most models of pancreatic lipase activity, colipase functions to anchor lipase on the substrate int
44 pase-lipase complex at an interface and that colipase has a function in lipolysis in addition to anch
46 tion of the lipase cofactor, procolipase, to colipase has no consequence for intestinal lipolysis and
47 In the presence of bile salt micelles and colipase, human PLRP2 hydrolyzed long-chain tri-, di-, a
48 ry to the existing paradigm, the presence of colipase in a lipid monolayer was not sufficient to enab
50 pase and lipase suggest another function for colipase in maintaining the active conformation of lipas
53 phery and suggest that, together with lipase-colipase interaction, the fatty acid-rich nano-domain su
54 demonstrate that the hydrophilic surface of colipase interacts with PTL in solution to form active c
55 in the subphase, the surface excess of [14C]colipase is 29% higher than that of procolipase, indicat
57 e that Glu15 is critical for activity of the colipase-lipase complex at an interface and that colipas
58 ity demonstrated in this study suggests that colipase may regulate the type of surfaces to which coli
60 rically over this range of compositions, the colipase molecules should be separated by up to 0-2 acyl
61 the mutations decreased the affinity of the colipase mutants for PTL and prevented the formation of
62 hexapeptide fused to the carboxyl domains of colipase or dickkopf are devoid of biological activity.
66 To test this hypothesis, mixed monolayers of colipase, phosphatidylcholine, and fatty acid at the arg
69 nteracts with PTL in solution to form active colipase.PTL complexes, that bile salt micelles influenc
71 ved with the fatty acid which at lipid chain:colipase ratios >25 induces higher levels of colipase ad
72 also remains in the interface at lipid chain:colipase ratios >3 but shows little additional interacti
78 ample, with diacylphosphatidylcholine alone, colipase remained in the lipid monolayer at surface pres
80 yceride lipase (PTL) showed that there was a colipase-stimulated REH activity in rat and mouse (WT an
82 s tested by measuring the adsorption of [14C]colipase to monolayers of 1-stearoyl-2-oleoyl-sn-3-glyce
83 tro, pancreatic triglyceride lipase requires colipase to restore activity in the presence of inhibito
84 orption over that observed in the absence of colipase was dependent on the fatty acid and colipase mo
86 nteraction of the pancreatic lipase cofactor colipase with a diacylphosphatidylcholine, acylglycerols
87 binding, and that the proper interaction of colipase with PTL requires the Glu(64)/Arg(65) binding s
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