Detection of rViscumin in plasma samples by immuno-PCR

Adler, Michael; Langer, Martin; Witthohn, Klaus; Eck, Jürgen; Blohm, Dietmar; Niemeyer, Christof M.

doi:10.1016/s0006-291x(02)02912-1

Cited by 46 publications

(48 citation statements)

References 12 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Methods were developed based principally on immunoassays [208] and mass spectrometry analysis [209]. An immuno-PCR set up for the determination of viscumin [210] could also be employed. Furthermore, research on antibodies [211] and vaccines [212][213][214][215] has been performed to afford protection against ricin, with emphasis on the protection against the inhaled toxin [216].…”

Section: Bioweaponsmentioning

confidence: 99%

Ribosome-inactivating proteins: progress and problems

Stirpe

Battelli

2006

Cell. Mol. Life Sci.

321

225

View full text Add to dashboard Cite

Ribosome-inactivating proteins (RIPs), mostly from plants, are enzymes which depurinate rRNA, thus inhibiting protein synthesis. They also depurinate other polynucleotide substrates. The biological activity of RIPs is not completely clarified, and sometimes independent of the inhibition of protein synthesis. There are differences in the cytotoxicity of RIPs and, consequently, in their toxicity to animals. Some RIPs are potent toxins, the best known being ricin, a potential biological weapon. New toxins have recently been identified. RIPs cause apoptotic and necrotic lesions, and induce production of cytokines causing inflammation. RIPs are potentially useful in agriculture and medicine because (i) they have antiviral activity and (ii) they are used for the preparation of conjugates with antibodies ('immunotoxins') or other carriers, rendering them specifically toxic to the cell target of the carrier, which may be helpful in therapy. The distribution, mechanism of action and role in nature of RIPs are not completely understood, and we can expect several future developments in their practical application.

show abstract

Section: Bioweaponsmentioning

confidence: 99%

Ribosome-inactivating proteins: progress and problems

Stirpe

Battelli

2006

Cell. Mol. Life Sci.

321

225

View full text Add to dashboard Cite

show abstract

“…IPCR was recently adapted to the detection of Aviscumine in samples of human plasma [7]. Aviscumine (rViscumin) is a heterodimeric 57 kDa recombinant mistletoe lectin (rML) [8,9], heterologously expressed in Escherichia coli-based on the genetic information of plant-derived lectin, which belongs to the type II ribosome inactivating protein (RIP)-family.…”

Section: Introductionmentioning

confidence: 99%

Adaptation and performance of an immuno-PCR assay for the quantification of Aviscumine in patient plasma samples

Adler¹,

Langer²,

Witthohn³

et al. 2005

Journal of Pharmaceutical and Biomedical Analysis

Self Cite

View full text Add to dashboard Cite

“…Recently, the technique to detect nML I-III in nanogram ranges in human serum has been developed [11,12]. A recombinant type II ribosome inactivating protein (rML) analogous to natural mistletoe lectin I revealed a short half life of about 13 minutes in cancer patients [12].…”

Section: Page 18 Of 42 European Journal Of Clinical Pharmacologymentioning

confidence: 99%