trichokirin/trichosanthes

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[Purification and characterization of trichokirin-S1, a novel ribosome-inactivating peptide from seeds of Trichosanthes kirilowii].

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A novel peptide from the seeds of Trichosanthes kirilowii, trichokirin-S1, was purified by extraction of protein body, ammonia sulfate precipitation, Blue-gel affinity chromatography, FPLC Mono S ion exchange chromatography and Superose12 gel filtration chromatography. Its molecular weight was

Purification and Partial Characterization of S-trichokirin, A New Small Ribosome-inactivating Protein, from Seeds of Trichosanthes kirilowii.

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A new small ribosome-inactivating protein named S-trichokirin from the seeds of Trichosanthes kirilowii was purified by ammonia sulfate precipitation, CM-52 ion exchange chromatography, Sephacryl S-100 gel filtration and FPLC Mono S ion exchange chromatography. S-trichokirin has molecular weight

Preparation and preliminary application of monoclonal antibodies against Trichokirin-S1, a small ribosome-inactivating peptide from the seeds of Trichosanthes kirilowii.

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Trichokirin-S1, a small ribosome-inactivating peptide recently purified from the seeds of Trichosanthes kirilowii, has potential clinical applications because of its small molecular mass. Two stable strains of hybridomas (1F11 and 2A5) that can secrete highly specific monoclonal antibodies (mAbs)

Trichokirin, a ribosome-inactivating protein from the seeds of Trichosanthes kirilowii Maximowicz. Purification, partial characterization and use for preparation of immunotoxins.

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A protein, here named trichokirin, was extracted from the seeds of Trichosanthes kirilowii and purified by ion-exchange and gel-filtration chromatography. Trichokirin is a basic glycoprotein of apparent relative molecular mass of 27,000 with a strong ribosome-inactivating activity. Alignment of the

Isolation and characterization of a novel ribosome-inactivating protein, beta-kirilowin, from the seeds of Trichosanthes kirilowii.

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A novel ribosome-inactivating protein designated beta-kirilowin was isolated from the seeds of Trichosanthes kirilowii. The proteins exhibited strong abortifacient activity in pregnant mice and produced a single band after SDS-polyacrylamide gel electrophoresis with an apparent mol. wt. of 27,500

alpha-Kirilowin, a novel ribosome-inactivating protein from seeds of Trichosanthes kirilowii (family Cucurbitaceae): a comparison with beta-kirilowin and other related proteins.

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A novel ribosome-inactivating protein (RIP) designated alpha-kirilowin was isolated from the seeds of Trichosanthes kirilowii. The molecular weight of alpha-kirilowin was estimated by SDS-polyacrylamide gel electrophoresis to be 28 800 Da, which is slightly larger than another previously

Some ribosome-inactivating proteins depurinate ribosomal RNA at multiple sites.

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Saporin-S6, a ribosome-inactivating protein (RIP) from Saponaria officinalis released more than 1 mol of adenine/mol of ribosomes from house fly (Musca domestica) larvae and from rat liver. The release of adenine from rat liver ribosomes by several RIPs (plant enzymes with RNA N-glycosidase

Ribosome-inactivating Proteins from Root Tubers and Seeds of Trichosan-thes kirilowii and Other Trichosanthes Species.

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Ribosome-inactivating proteins have been isolated from Trichosanthes kirilowii root tubers and seeds, including trichosanthin, karasurin and T 33 from root tubers and trichosanthrip, trichokirin, alpha-kirilowin, beta-kirilowin and trichoanguin from seeds. The aforementioned proteins show structural

Trichosanthin-monoclonal antibody conjugate specifically cytotoxic to human hepatoma cells in vitro.

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A plant single-chain ribosome-inactivating protein derived from the root tuber of Trichosanthes kirilowii, termed trichosanthin (TCS), was modified with 2-iminothiolane. It was not like trichokirin, a ribosome-inactivating protein derived from the seeds of the same plant, in that TCS retained full

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