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91 results for “lipases”
Fig. 4 in Mobilization of storage lipid reserve and expression analysis of lipase and lipoxygenase genes in rice (Oryza sativa var. Pusa Basmati 1) bran during germination
Fig. 4. Exon/intron organization of (a) OsLip genes [Exons (green boxes), Introns (red lines)] and (b) OsLOX genes [Exons (pink boxes), Introns (grey lines)]. (For interpretation of the references to color in this figure legend, the reader is referred to the Web version of this article.)
Fig. 3 in Mobilization of storage lipid reserve and expression analysis of lipase and lipoxygenase genes in rice (Oryza sativa var. Pusa Basmati 1) bran during germination
Fig. 3. Phylogenetic analysis of rice LOXs. Neighbor-joining (NJ) estimates (with 1000 bootstrap replicates) the phylogenetic relationship between rice and Arabidopsis LOX proteins. Labels are depicted in green for the 9-LOX clade, in blue for 13-LOX clade. Bootstrap values are mentioned in the branches. Branch length is indicated by the scale bar. The Arabidopsis Information Resource (TAIR) and Rice genome annotation project (RGAP) accession numbers are indicated with species names of the lipase proteins. Os, Oryza sativa; At, Arabidopsis thaliana. (For interpretation of the references to color in this figure legend, the reader is referred to the Web version of this article.)
Fig. 2 in Mobilization of storage lipid reserve and expression analysis of lipase and lipoxygenase genes in rice (Oryza sativa var. Pusa Basmati 1) bran during germination
Fig. 2. Phylogenetic analysis of rice lipases (Lip). Neighbor-joining (NJ) estimates (with 1000 bootstrap replicates) the phylogenetic relationship between rice and Arabidopsis lipase proteins. AtLip are depicted in green box and six OsLip candidates selected for the study based on the tree are depicted in blue box. Bootstrap values are mentioned in the branches. Branch length is indicated by the scale bar. The Arabidopsis Information Resource (TAIR) and Rice genome annotation project (RGAP) accession numbers are indicated with species names of the lipase proteins. Os, Oryza sativa; At, Arabidopsis thaliana; SDP1, sugar dependent1. (For interpretation of the references to color in this figure legend, the reader is referred to the Web version of this article.)
Efficacy and Safety of Bile Salt Stimulated Lipase (BSSL) as Replacement Therapy in Pasteurized Breast Milk for Preterm Infants
ClinicalTrials.gov study NCT00659243. IPD Sharing: Not stated. Countries: 2. Publications: 1.
Efficacy and Safety of Bile Salt Stimulated Lipase (BSSL) as Replacement Therapy in Infant Formula for Preterm Infants
ClinicalTrials.gov study NCT00658905. IPD Sharing: Not stated. Countries: 1. Publications: 1.
Effect of Dietary Components on Gastrointestinal Side Effects Induced by Orlistat, a Lipase Inhibitor
ClinicalTrials.gov study NCT01320228. IPD Sharing: Not stated. Countries: 1. Publications: 1.
Study to Re-assess and Re-confirm Data Previously Recorded About the Incidence and Severity of Acute Abdominal "Pancreatitis" Episodes in Lipoprotein Lipase Deficient (LPLD) Subjects Previously Enroll
ClinicalTrials.gov study NCT01448577. IPD Sharing: Not stated. Countries: 1. Publications: 3.
National Lysosomal Acid Lipase Deficiency Study
ClinicalTrials.gov study NCT02372513. IPD Sharing: Not stated. Countries: 1. Publications: 14.
Lysosomal Acid Lipase (LAL) Deficiency Registry
ClinicalTrials.gov study NCT01633489. IPD Sharing: NO. Countries: 22. Publications: 3.
Effect of Candida Rugosa Lipase on Serum Triglyceride Lowering
ClinicalTrials.gov study NCT05295134. IPD Sharing: NO. Countries: 1. Publications: 2.
Efficacy and Safety of Human Lipoprotein Lipase (LPL)[S447X] Expressed by an Adeno-Associated Viral Vector in LPL-deficient Subjects
ClinicalTrials.gov study NCT00891306. IPD Sharing: Not stated. Countries: 1. Publications: 6.
An Observational Study of Patients With Lysosomal Acid Lipase Deficiency/Cholesteryl Ester Storage Disease Phenotype
ClinicalTrials.gov study NCT01528917. IPD Sharing: NO. Countries: 8. Publications: 2.
Safety and Efficacy in LPL-Deficient Subjects of AMT-011, an Adeno-Associated Viral Vector Expressing Human Lipoprotein Lipase [S447X]
ClinicalTrials.gov study NCT01109498. IPD Sharing: Not stated. Countries: 1. Publications: 7.
Data from: Novel amphiphilic polyvinylpyrrolidone (PVP) functionalized silicone particles as carrier for low cost lipase immobilization
The high catalytic activity, specificity and stability of immobilization lipase have been drawn a great interests. How to reduce the cost of support materials has always been a hot topic in this field. Herein, for the development of low-cost immobilized lipase, we demonstrate an amphiphilic polyvinylpyrrolidone (PVP) grafted on silicone particles (SP) surface materials (SP-PVP) with rational design based on interfacial activation and solution polymerization. Meanwhile, the hydrophilic pristine SP and hydrophobic polystyrene-corded silicone particles (SP-Pst) were also prepared for lipase immobilization. The SP-PVP were characterized by X-ray diffraction, scanning electron microscopy, X-ray photoelectron spectroscopy, Fourier transforms infrared spectroscopy and thermogravimetry. Our results indicated that the lipase loading amount on the SP-PVP composites was about 215 mg of protein per g. In the activity assay, the immobilized lipase SP-PVP@CRL exhibited higher catalysis activity, better thermostability and reusability than that of SP@CRL and SP-Pst@CRL. The immobilized lipase retained more than 54 % of its initial activities after 10 times reuse and approximately trended to a steady in the following cycles. By introducing the interesting amphiphilic polymer to these cheap and easily obtained silicone particles (SP) surface, the relative performance of immobilized lipase can be significantly improved, rendering interactions between the low cost supports materials and lipase.
Figures 1-4 from: Gottlieb Almeida AP, Zardo EL, Toni C, Behr ER, Picolli da Silva L, Vieira JP, Loro VL, Baldisserotto B (2018) Composition of gastrointestinal content, protease and lipase activities in summer and winter of four freshwater siluriforms (Teleostei: Actinopterygii) with two different feeding habits. Zoologia 35: 1-8. https://doi.org/10.3897/zoologia.35.e13286
Figures 1-4 Species used in the analysis: (1) Rhamdia quelen; (2) Pimelodus maculatus; (3) Loricariichthys anus; (4) Hypostomus commersoni. Figures 1, 2 and 4 kindly provided by Alexssandro G. Becker and figure 3 by Luiz R. Malabarba.
Figures 10-11 from: Gottlieb Almeida AP, Zardo EL, Toni C, Behr ER, Picolli da Silva L, Vieira JP, Loro VL, Baldisserotto B (2018) Composition of gastrointestinal content, protease and lipase activities in summer and winter of four freshwater siluriforms (Teleostei: Actinopterygii) with two different feeding habits. Zoologia 35: 1-8. https://doi.org/10.3897/zoologia.35.e13286
Figures 10-11 Lipase activity in the omnivorous R. quelen and P. maculatus and detritivorous L. anus and H. commersoni in the summer and winter: (10) anterior intestine; (11) posterior intestine. Different letters indicate significant differences between species in the same season. * Indicates a significant difference from the summer in the same segment (p < 0.05). (U, a Caraway unit) (n = 15 from each species at each season).
Figures 5-9 from: Gottlieb Almeida AP, Zardo EL, Toni C, Behr ER, Picolli da Silva L, Vieira JP, Loro VL, Baldisserotto B (2018) Composition of gastrointestinal content, protease and lipase activities in summer and winter of four freshwater siluriforms (Teleostei: Actinopterygii) with two different feeding habits. Zoologia 35: 1-8. https://doi.org/10.3897/zoologia.35.e13286
Figures 5-9 Proteolytic enzymatic activities in the omnivorous R. quelen and P. maculatus and detritivorous L. anus and H. commersoni in the summer and winter: (5) pepsin in the stomach; (6) trypsin in the anterior intestine; (7) trypsin in the posterior intestine; (8) chymotrypsin in the anterior intestine; (9) chymotrypsin in the posterior intestine. Different letters indicate significant differences between species in the same season. * Indicates a significant difference from summer in the same segment (p < 0.05). (U, a Caraway unit) (n = 15 from each species at each season).
lipase_docking_socore
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Fig. 1 in Screening of in vitro and in silico α-amylase, α-glucosidase, and lipase inhibitory activity of oxyprenylated natural compounds and semisynthetic derivatives
Fig. 1. Chemical structures of the 23 analysed pure natural and semisynthetic compounds.
Cholinesterase, Amylase, Lipase and Neutrophil-to-lymphocyte Ratio in Acute Pesticide Poisoning Cases
ClinicalTrials.gov study NCT05310188. IPD Sharing: Not stated. Countries: 0. Publications: 5.
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