To allow for pharmacokinetic studies in adjunction with the current clinical developments of the potent cytostatic anti-cancer drug rViscumin, a sandwich immuno-PCR (IPCR) assay was developed for the detection of rViscumin in blood plasma. The IPCR was carried out with a commercially available reagent kit, consisting of pre-assembled rViscumin-specific antibody-DNA conjugates as well as a specific competitor DNA fragment to be amplified by PCR. Various combinations of capture- and detection-antibodies were compared for performance in IPCR. Using the optimized assay, as few as 50 zeptomol (approx. 100 fg/ml) rViscumin (MW 57 kDa) was detectable in standardized human serum samples. The IPCR assay was very selective for rViscumin and in spiking experiments in proband plasma samples, signal recovery rates between 70% and 120% were obtained. The linear sensitivity range of the assay covered more than five orders of magnitude. Repeated measurements of rViscumin resulted in a mean standard deviation value of 14.2%.
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http://dx.doi.org/10.1016/s0006-291x(02)02912-1 | DOI Listing |
Biochimie
November 2022
Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, 16/10 Miklukho-Maklaya str., Moscow, 117997, Russia; Faculty of Biology and Biotechnology, HSE University, 33 b.4 Profsoyuznaya str., Moscow, 117418, Russia.
Viscumin, a lectin used in anti-cancer therapy, was originally considered as βGal recognizing protein; later, an ability to bind 6'-sialyl N-acetyllactosamine (6'SLN) terminated gangliosides was found. Here we probed viscumin with a printed glycan array (PGA) containing a large number of mammalian sulfated glycans, and found a strong binding to glycans with 6-O-SuGal moiety as lactose, N-acetyllactosamine (LN), di-N-acetyllactosamine (LacdiNAc), and even 6-O-SuGalNAcα (but not SiaTn). Also, the ability to bind some of αGal terminated glycans, including Galα1-3Galβ1-4GlcNAc, was observed.
View Article and Find Full Text PDFAnal Chim Acta
April 2020
Food and Drug Laboratory Research Center, Food and Drug Organization, Ministry of Health and Medical Education, P.O. Box 11136-15911, Tehran, Iran. Electronic address:
Viscum album lectin 1 (Viscumin) is one of the most important plant-based protein of potential adjuvant in cancer treatment. Therefore, the use of nano-biosensor technology as a novel emerges of biosensors is crucial to detect this modal agent in pharmacological study. Molecular imprinted polymer using 9-mer peptides sequence (epitope) was applied as a template.
View Article and Find Full Text PDFAnal Chem
January 2015
Swedish Defence Research Agency (FOI), CBRN Defence and Security , SE-901 82 Umeå, Sweden.
Type 2 ribosome-inactivating protein toxins (RIP-II toxins) were enriched and purified prior to enzymatic digestion and LC-MS analysis. The enrichment of the RIP-II family of plant proteins, such as ricin, abrin, viscumin, and volkensin was based on their affinity for galactosyl moieties. A macroporous chromatographic material was modified with a galactose-terminated substituent and packed into miniaturized columns that were used in a chromatographic system to achieve up to 1000-fold toxin enrichment.
View Article and Find Full Text PDFJ Pharm Biomed Anal
January 2007
Institut für Pharmazeutische Technologie, Technische Universität Braunschweig, Mendelssohnstr. 1, 38106 Braunschweig, Germany.
Extracts from Viscum album leaves, with mistletoe lectin I (ML I) as the main therapeutic agent, are commonly used as an immunomodulating adjuvat in tumour therapy. Because of its popularity against cancer and the possibility for a better standardisation a recombinant ML I (rML I) was developed by Eck et al. To improve the sensitivity of an already established enzyme linked lectin assay (ELLA) for rML I human haptoglobins with different phenotypes (1.
View Article and Find Full Text PDFActa Crystallogr Sect F Struct Biol Cryst Commun
January 2005
Institute of Biochemistry and Food Chemistry, University of Hamburg, c/o DESY, Notkestrasse 85, 22603 Hamburg, Germany.
The structures of mistletoe lectin I (ML-I) from Viscum album complexed with lactose and galactose have been determined at 2.3 A resolution and refined to R factors of 20.9% (Rfree = 23.
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