about
Mutational analysis of a blood coagulation factor VIII-binding peptide.Evaluation of a sensitive detection method for peptide arrays prepared by SPOT synthesis.Monoliths for fast bioseparation and bioconversion and their applications in biotechnology.Polymethacrylate monoliths for preparative and industrial separation of biomolecular assemblies.Ion-exchange chromatography.Secretory immunoglobulin purification from whey by chromatographic techniques.Impact of sulfur and vitamin C on the allergenicity of Mal d 2 from apple (Malus domestica).Matrix-assisted refolding of autoprotease fusion proteins on an ion exchange column: a kinetic investigation.Refolding of Npro fusion proteins.N(pro) fusion technology to produce proteins with authentic N termini in E. coli.Cytokine activity assay by means of proliferation measured in plane convex microtiter wells.Matrix-assisted refolding of autoprotease fusion proteins on an ion exchange column.Affinity monoliths generated by in situ polymerization of the ligand.Continuous processing of recombinant proteins: Integration of inclusion body solubilization and refolding using simulated moving bed size exclusion chromatography with buffer recycling.Dispersion effects in preparative polymethacrylate monoliths operated in radial-flow columns.Identification and deletion of the major secreted protein of Pichia pastoris.Continuous processing of recombinant proteins: integration of refolding and purification using simulated moving bed size-exclusion chromatography with buffer recycling.A nonchromatographic process for purification of secretory immunoglobulins from caprine whey.Comparison of protein A affinity sorbents.Autoprotease N(pro): analysis of self-cleaving fusion protein.Prediction of inclusion body solubilization from shaken to stirred reactors.A systematic evaluation of mechanisms, material effects, and protein-dependent differences on friction-related protein particle formation in formulation and filling steps.High-throughput system for determining dissolution kinetics of inclusion bodies.A microscale method of protein extraction from bacteria: Interaction of Escherichia coli with cationic microparticles.Integrated continuous dissolution, refolding and tag removal of fusion proteins from inclusion bodies in a tubular reactor.Mapping ofMalus domestica allergens by 2-D electrophoresis and IgE-reactivityHigh level expression of a promising anti-idiotypic antibody fragment vaccine against HIV-1 in Pichia pastorisPeak broadening in protein chromatography with monoliths at very fast separationsHydrophobic interaction chromatography of proteins. II. Binding capacity, recovery and mass transfer propertiesA simple method to quantify staphylococcal protein A in the presence of human or animal IgG in various samplesControl method for integrity of continuous bedsBovine whey fractionation based on cation-exchange chromatographyHydrophobic interaction chromatography of proteins. I. Comparison of selectivityHydrophobic interaction chromatography of proteins IV. Kinetics of protein spreadingPerformance and characterization of a nanophased porous hydroxyapatite for protein chromatographyHydrophobic interaction chromatography of proteins. III. Unfolding of proteins upon adsorptionMass transfer characteristics of plasmids in monolithsComparison of protein A affinity sorbents II. Mass transfer propertiesHydrophobic interaction chromatography of proteins V. Quantitative assessment of conformational changesIn situ determination of adsorption kinetics of proteins in a finite bath
P50
Q30833859-FB22CE0B-E84B-408A-8043-0464D99D36ACQ33232561-BA9E3B23-AB12-4A3C-909E-B51375856E09Q35881454-54033655-5D26-4973-A846-D0BC090AA866Q37074492-578F06A2-11E4-42CE-84E7-D1C7F6BCFF3AQ37628087-A028B5D5-E555-4E14-A1C6-AA0B1772CB2EQ38672761-88AF038C-3556-4B60-AF35-F4C48E699D7AQ38979145-F39C1E6D-FA0E-4247-8A20-9BCC15DAF4F1Q40351323-3CA461E5-C024-4C65-99B3-1EAF396A14B8Q40384896-C55D9F8B-89EB-417E-97C0-97F1CECEE2D4Q40434025-2A029A0C-5707-427A-8445-9B433730A89FQ41198934-0F93C49C-0507-4BDA-85A2-092E24FB7CACQ43255524-DC70C86A-0A91-41DA-917F-DEB97D82C0E8Q43808098-215FAF5F-B39A-4FDF-B077-A89F945D0836Q43878164-1BC7F4D5-4989-4EE8-932C-51BAF4635336Q43957950-01115C43-8966-4B13-805C-A88668749CACQ46057265-DE50566F-9572-4D04-8BC3-E15F383AA9F4Q47178757-66B0731B-98B2-438B-A3AA-97F5AC24F361Q47401507-69FB5078-B14D-4997-AB99-2A10CF903587Q47886450-A2A6DAA0-A977-410F-B817-B898C88E67ABQ47973555-0D87BFA2-2141-4FC4-9CE5-986DB51E8DC0Q47995410-6E0880FE-F7F0-408B-8887-A837E4A98838Q51589098-A1B701BE-EC6E-4386-AD97-AE831F3A43F6Q51767563-BE8390E3-5302-4545-A1E1-5CAF94DABF0CQ52659913-CC1769EA-54F1-470C-8083-71BD6CCFE49CQ53520844-6BF0A234-A5A0-4CB1-B3DA-E5A06FA1BFA7Q59386573-52966080-E8E6-4B60-9947-AEC4AFEAC821Q61554381-33DB4E73-9769-409C-9335-9E021F53DC55Q73133706-90C9D554-9A61-4FF3-8F3D-A617D80886E6Q73437797-C6A587D6-1F4B-4DC8-8D69-647F5E75589CQ73450904-668C1369-3446-442A-8E60-68691ECD4066Q73539376-EE650315-B037-4E1B-9271-7D395792DFD1Q74401993-3E918B75-3A20-41A8-B4AA-AD4F6A691EFFQ78415851-20E6F909-0762-4155-B9BB-295801B9B4D8Q79372104-3CC059CD-DED1-416C-96FB-1E1C95FB2F94Q80389880-5F05C3F0-7BDE-491C-84F7-4F74F183FAFFQ80413967-B259D3D1-7E3D-4A09-9D7A-37458A498DADQ80539633-359757CE-B266-437F-AE92-C2908705483EQ81369410-88638D31-BDCE-44CD-A97D-115373058395Q81425801-40E7A3A8-039D-4EB8-93E9-BAABB7247E16Q81673953-4E59C34C-3CE7-4A23-A866-218AB27BC19C
P50
description
hulumtues
@sq
onderzoeker
@nl
researcher
@en
հետազոտող
@hy
name
Rainer Hahn
@ast
Rainer Hahn
@en
Rainer Hahn
@es
Rainer Hahn
@sl
type
label
Rainer Hahn
@ast
Rainer Hahn
@en
Rainer Hahn
@es
Rainer Hahn
@sl
prefLabel
Rainer Hahn
@ast
Rainer Hahn
@en
Rainer Hahn
@es
Rainer Hahn
@sl
P106
P1153
7202700762
P21
P31
P496
0000-0001-5654-5032