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ricin/sarcoma

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The uptake of adriamycin (Adm) by normal tissues and by sarcomas transplanted to both kidneys in rats was studied at 10 min following constant rate infusion of Adm 5 mg/kg body wt into one renal artery, during 3 and 10 min. Since the selectively infused kidney extracted only about 20% of the total
The potential use of tumour-specific T-lymphocytes loaded with ricin in cell targeting experiments was investigated. Moloney-murine sarcoma virus (M-MSV)-specific T-lymphocytes, obtained in mass mixed leucocyte-tumour cell culture (MLTC) and a M-MSV-specific cytotoxic T-lymphocyte (CTL) clone, were

[Necrosing or clastic effects of ricin on different organs and on experimental sarcomas].

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Ricin toxin A chain (RTA) was conjugated to monoclonal antibody 791T/36, which was raised originally against human osteogenic sarcoma cell line 791T. The resultant conjugates were characterized and tested for cytotoxicity against a panel of human tumor cell lines representing a defined range of

Phase I study of the plant protein ricin.

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A Phase I study was carried out with ricin, a plant toxin acting by inhibiting protein synthesis, on 54 cancer patients with advanced disease. Ricin was given as i.v. bolus injections every two weeks at dose levels ranging from 4.5 to 23 micrograms/sq m of estimated body surface area. Ricin was well
We developed a model to assess the therapeutic effects of the 45-2D9-ricin A-chain immunotoxin (RTA) on pulmonary metastases. The 45-2D9 mouse monoclonal antibody recognizes a Mr 74,000 glycoprotein highly expressed by rat fibroblasts transformed with the Kirsten sarcoma virus (transformed rat
An immunotoxin comprising a tumour-specific monoclonal antibody (11/160) coupled to ricin A chain, although inactive in in vitro cytotoxicity assays against HSNtc sarcoma target cells, was found to be capable of significant tumouricidal activity in syngeneic rats if potentiated by ricin B chain. The

Binding and cytotoxicity of Ricinus communis lectins to HeLa cells, Sarcoma 180 ascites tumor cells and erythrocytes.

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The binding of Ricinus communis lectins to HeLa cells, Sarcoma 180 ascites tumor cells and human erythrocytes was studied in detail. Scatchard plots of binding of 125I-lectins to these cells gave biphasic lines except for HeLa cells at 0 degree C. The association constants of lectins for the three

Monoclonal antibody-ricin A chain conjugates (immunotoxins): potential therapeutic agents for human colon carcinoma.

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With the advent of hybridoma technology, monoclonal antibodies (MAbs) can be produced against specific human tumor cell-surface antigens. 44X14, an MAb produced in our laboratory by the immunization of BALB/c mice with colon carcinoma cells, exhibits high affinity for breast, lung, and colon
The immunoconjugate XMMCO-791/RTA consists of ricin A chain bound to a murine monoclonal antibody MoAb 791T. This monoclonal antibody (MoAb) binds to a glycoprotein of 72 kD, which is expressed on human colorectal carcinoma, ovarian carcinoma, and osteogenic sarcoma. XMMCO-791/RTA was tested in a

Endocytosis of immunotoxin-791T/36-RTA by tumor cells in relation to its cytotoxic action.

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Ricin A chain immunotoxin constructed with monoclonal antibody 791T/36, which recognizes a tumor associated glycoprotein Mr 72,000 antigen present on sarcomas and colon and ovarian cancer cells, is cytotoxic for cell lines from tumors expressing this antigen. Incubation of sarcoma 791T cells with

Lectin derivatives of methotrexate and chlorambucil as chemotherapeutic agents.

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Methotrexate and chlorambucil, each covalently linked to either abrus agglutinin, abrin, ricinus agglutinin, ricin, or concanavalin A, were prepared. A single dose of the derivative injected ip into sarcoma 180-bearing noninbred N:NIH(S) white mice resulted in prolongation of the survival time and

Immunochemical characterization of fetal antigen isolated from spent medium of a human melanoma cell line.

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A fetal antigen (FA) was isolated from spent culture medium of a melanoma (M14) cell line. Allogeneic serum samples from melanoma patients, previously characterized with respect to anti-FA activity, were used as the source of anti-FA antibody. The FA activity was partially purified by membrane
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