Search results for " Site-Directed"

showing 2 items of 132 documents

A targeted apoB38.9 mutation in mice is associated with reduced hepatic cholesterol synthesis and enhanced lipid peroxidation.

2006

Familial hypobetalipoproteinemia (FHBL) due to truncation-specifying mutations of apolipoprotein B (apoB), which impair hepatic lipid export in very low-density lipoprotein (VLDL) particles, is associated with fatty liver. In an FHBL-like mouse with the apoB38.9 mutation, fatty liver develops despite reduced hepatic fatty acid synthesis. However, hepatic cholesterol contents in apoB38.9 mice are normal. We found that cholesterogenic enzymes (3-hydroxy-3-methylglutaryl-coenzyme A reductase, sterol-C5-desaturase, and 7-dehydrocholesterol reductase) were consistently downregulated in two separate expression-profiling experiments using a total of 19 mice ( n = 7 each for apob+/+and apob+/38.9, …

medicine.medical_specialtyVery low-density lipoproteinApolipoprotein BPhysiologymedicine.disease_causeLipid peroxidationHypobetalipoproteinemiaschemistry.chemical_compoundMicePhysiology (medical)Internal medicineNAFLDmedicineAnimalsFamilial hypobetalipoproteinemiamice modelCells CulturedApolipoproteins BMutationHepatologybiologyChemistryMutagenesisGastroenterologyGene targetingRatsFatty LiverMice Inbred C57BLEndocrinologyCholesterolLiverApolipoprotein B-100Gene Targetingbiology.proteinHepatocytesMutagenesis Site-Directedlipids (amino acids peptides and proteins)Lipid PeroxidationmutationOxidative stressLipoproteinAmerican journal of physiology. Gastrointestinal and liver physiology
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A single mutation in the recombinant light chain of tetanus toxin abolishes its proteolytic activity and removes the toxicity seen after reconstituti…

1994

Specific proteolysis by the tetanus toxin light chain of a vesicle-associated membrane protein (VAMP) involved in exocytosis is thought to underlie its intracellular blockade of neurotransmitter release. To substantiate this mechanism, recombinant light chain was expressed as a maltose binding protein-light chain fusion product in Escherichia coli. After purification of affinity chromatography and cleavage with factor Xa, the resultant light chain was isolated and its identity confirmed by Western blotting and N-terminal sequencing. It exhibited activity similar to that of the native light chain in proteolyzing its target in isolated bovine small synaptic vesicles and in hydrolyzing a 62-re…

medicine.medical_treatmentRecombinant Fusion ProteinsMolecular Sequence DataNeurotoxinsGlutamic AcidMaltose bindingNerve Tissue ProteinsIn Vitro TechniquesImmunoglobulin light chainBiochemistrySynaptic vesicleExocytosislaw.inventionR-SNARE ProteinsMiceStructure-Activity RelationshipAffinity chromatographyGlutamatesTetanus ToxinlawThermolysinEndopeptidasesmedicineEscherichia coliAnimalsAmino Acid SequenceProteaseBase SequenceChemistryMembrane ProteinsMolecular biologyPeptide FragmentsRecombinant DNAMutagenesis Site-DirectedCattleBiochemistry
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