Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Multi-step purification strategy for RANTES wild-type and mutated analogues expressed in a baculovirus system.

Journal of chromatography. B, Biomedical sciences and applications - 14 Jan 2000

Comuzzi B, Arcelloni C, Polo S, Nardese V, Lusso P, Paroni R

Abstract excerpt

RANTES (regulated on activation, normal T cell expressed and secreted), a C-C chemokine, is one of the major HIV-suppressive factors produced by CD8+ T cells. Wild-type RANTES and genetically modified analogues were expressed in a baculovirus system and purified from cell culture supernatants employing a multi-step strategy based on affinity and RP-HPLC. Quantification and purity control of the final proteins...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Baculoviridae
Share to Chemokine CCL5

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Chromatography, Affinity

Share to Chromatography, High Pressure Liquid

Share to Electrophoresis, Capillary

Share to Enzyme-Linked Immunosorbent Assay

Share to Mass Spectrometry

Share to Recombinant Proteins

Source

Identifiers

PMID: 10681040
DOI: 10.1016/s0378-4347(99)00361-8

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Multi-step purification strategy for RANTES wild-type and mutated analogues expressed in a baculovirus system.PMID 10681040Read ↗

Structural and functional studies of the potent anti-HIV chemokine variant P2-RANTES.Semantic proximity Read ↗

Engineering the glycosaminoglycan-binding affinity, kinetics and oligomerization behavior of RANTES: a tool for generating chemokine-based glycosaminoglycan antagonists.Semantic proximity Read ↗

The superior folding of a RANTES analogue expressed in lactobacilli as compared to mammalian cells reveals a promising system to screen new RANTES mutants.Semantic proximity Read ↗

Peptide affinity chromatography media that bind N(pro) fusion proteins under chaotropic conditions.Semantic proximity Read ↗

Overexpression, Purification and Functional Characterisation of Wild-Type HIV-1 Subtype C Protease and Two Variants Using a Thioredoxin and His-Tag Protein Fusion System.Semantic proximity Read ↗

Aggregation of RANTES is responsible for its inflammatory properties. Characterization of nonaggregating, noninflammatory RANTES mutants.Semantic proximity Read ↗

Human immunodeficiency virus type 1 entry inhibitors selected on living cells from a library of phage chemokines.Semantic proximity Read ↗

Capillary electrophoresis of recombinant proteins.Semantic proximity Read ↗

Limited and defined truncation at the C terminus enhances receptor binding and degranulation activity of the neutrophil-activating peptide 2 (NAP-2). Comparison of native and recombinant NAP-2 variants.Semantic proximity Read ↗

The BBXB motif of RANTES is the principal site for heparin binding and controls receptor selectivity.Semantic proximity Read ↗

Immunoaffinity Purification of the Glycosylated Extracellular Fragment of Mouse Plexin A2 Produced in a Mammalian Expression System.Semantic proximity Read ↗

Expression of recombinant human GM2-activator protein in insect cells: purification and characterization by mass spectrometry.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.