PubMed Health⌕ Search
Home/Archive/PubMed

PubMed · 10214699

Antibody purification methods.

M A Vijayalakshmi
View original source ↗Export metadata ↓

Abstract

Antibodies (Abs) from the sera of patients with autoimmune diseases are reported to have different catalytic functions. Their recovery by efficient purification methods is, therefore, a crucial step. This article reviews different available methods for their recovery and emphasizes a new approach, namely adsorbents with immobilized histidine, which allows a good purification both in yield and purity of Abs, with the additional advantage of using gentle elution conditions. This, in turn, will ensure the recovery of intact (nondenatured) catalytically functional Abs, directly from the sera.

Explore related subjects

AntibodiesAutoimmune DiseasesChromatography, AffinityHistidineHumansJournal ArticleReview

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

M A Vijayalakshmi. 1998. Antibody purification methods.. https://doi.org/10.1007/bf02787711

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related citations

PubMed2021

ERBB3 overexpression due to miR-205 inactivation confers sensitivity to FGF, metabolic activation, and liability to ERBB3 targeting in glioblastoma.

In glioblastoma (GBM), the most frequent and lethal brain tumor, therapies suppressing recurrently altered signaling pathways failed to extend survival. However, in patient subsets, specific genetic lesions can confer sensitivity to targeted agents. By exploiting an integrated model based on patient-derived stem-like cells, faithfully recapitulating the original GBMs in vitro and in vivo, here, we identify a human GBM subset (∼9% of all GBMs) characterized by ERBB3 overexpression and nuclear accumulation. ERBB3 overexpression is driven by inheritable promoter methylation or post-transcriptional silencing of the oncosuppressor miR-205 and sustains the malignant phenotype. Overexpressed ERBB3 behaves as a specific signaling platform for fibroblast growth factor receptor (FGFR), driving PI3K/AKT/mTOR pathway hyperactivation, and overall metabolic upregulation. As a result, ERBB3 inhibition by specific antibodies is lethal for GBM stem-like cells and xenotransplants. These findings highlight a subset of patients eligible for ERBB3-targeted therapy.

Antibodies↗
PubMed2003

Malignant mesothelioma growth inhibition by agents that target the VEGF and VEGF-C autocrine loops.

Malignant mesothelioma (MM) is a locally aggressive tumor that originates from the mesothelial cells of the pleural and sometimes peritoneal surface. Conventional treatments for MM, consisting of chemotherapy or surgery give little survival benefit to patients, who generally die within 1 year of diagnosis. Hence, there is an urgent need for the development of alternative therapies. Vascular endothelial growth factor (VEGF) is an autocrine growth factor for MM. The closely related molecule, VEGF-C, is also implicated in malignant mesothelioma growth. VEGF-C and its cognate receptor VEGFR-3 are co-expressed in mesothelioma cell lines. A functional VEGF-C autocrine growth loop was demonstrated in mesothelioma cells by targeting VEGF-C expression and binding to VEGFR-3. The ability of novel agents that reduce the levels of VEGF and VEGF-C to inhibit mesothelioma cell growth in vitro was assessed. Antisense oligonucleotide (ODN) complementary to VEGF that inhibited VEGF and VEGF-C expression simultaneously specifically inhibited mesothelioma cell growth. Similarly, antibodies to VEGF receptor (VEGFR-2) and VEGF-C receptor (VEGFR-3) were synergistic in inhibiting mesothelioma cell growth. In addition, a diphtheria toxin-VEGF fusion protein (DT-VEGF), which is toxic to cells that express VEGF receptors was very effective in inhibiting mesothelioma cell growth in vitro. These results indicate that targeting VEGF and VEGF-C simultaneously may be an effective therapeutic approach for malignant mesothelioma.

Antibodies↗
PubMed2003

Investigation of an antibody-ligase. Evidence for strain-induced catalysis.

Catalytic antibody 16G3, a peptide ligase with extended substrate scope has been characterized mechanistically exploiting a set of systematically designed perspective substrates 6-9, two of which, thioesters 8 and 9 act instead as inhibitors. Taken together the structure/activity relationships suggest a catalytic mechanism dependent on induction of strain, programmed via specific structural deviations between the hapten and the substrates. General mechanistic implications for de novo induced catalysis are presented.

Antibodies↗