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Håvard Loftheim

Researcher at University of Oslo

Publications -  7
Citations -  99

Håvard Loftheim is an academic researcher from University of Oslo. The author has contributed to research in topics: High-performance liquid chromatography & Hydrophilic interaction chromatography. The author has an hindex of 6, co-authored 7 publications receiving 95 citations.

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Ion‐pair mediated transport of angiotensin, neurotensin, and their metabolites in liquid phase microextraction under acidic conditions

TL;DR: It is proved that for all peptides the transport across the organic phase is mediated by heptane-1-sulphonic acid, and the optimal pH of the donor phase was found to be different for the peptides, which opens opportunities for selective sample preparation.
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Urinary proteomic shotgun approach for identification of potential acute rejection biomarkers in renal transplant recipients

TL;DR: In this paper, serial urine samples in the early post transplant phase from 6 patients with biopsy verified acute rejections and 6 age-matched controls without clinical signs of rejection were analyzed by shotgun proteomics.
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On-Line multitasking analytical proteomics: how to separate, reduce, alkylate and digest whole proteins in an on-Line multidimensional chromatography system coupled to MS.

TL;DR: An on-Line multidimensional system has been developed, consisting of pH gradient strong anion exchange chromatography of native proteins in the first dimension with subsequent trapping and on-column reduction/alkylation on C4 trap columns and RP separation of the alkylated protein in the second dimension followed by on- column tryptic digestion and electrospray MS detection.
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2-D hydrophilic interaction liquid chromatography-RP separation in urinary proteomics--minimizing variability through improved downstream workflow compatibility.

TL;DR: The optimized and "streamlined" complex method has shown potential for use in future urinary proteomic studies and was tested in an extensive proteomic experiment on a kidney-transplanted patient.
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Improving off-line accelerated tryptic digestion. Towards fast-lane proteolysis of complex biological samples.

TL;DR: It was shown that complex proteins like bovine serum albumin (BSA) need much longer time and elevated temperature to be digested to an acceptable level compared to smaller proteins like cytochrome c, and the digestion using immobilized trypsin beads was considerable less time consuming.