luffin/cucumis melo

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[Purification and partial characterization of luffin P1, a peptide with translational inhibitory activity and trypsin inhibitory activity, from seeds of Luffa cylindrica].

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A peptide, luffin P1, from seeds of Luffa cylindrica, was purified by ammonia sulfate precipitation, CM-52 ion exchange chromatography, Blue-gel affinity chromatography and FPLC Mono S ion exchange chromatography. Its molecular weight was 5226.5 as determined by MALDI-TOF-MS analysis. The sequence

Luffin-S--a small novel ribosome-inactivating protein from Luffa cylindrica. Characterization and mechanism studies.

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We purified and characterized a novel RIP (ribosome inactivating protein), Luffin-S from the seeds of Luffa cylindrica. Different from Luffin-A and B, which are RNA N-glycosidases with molecular weights of 27 and 28 kDa, respectively, Luffin-S has an M.W. of only approx. 10 kDa, much smaller than

Identification of lysine residue at or near active site of luffin-a, a ribosome-inactivating protein from seeds of Luffa cylindrica.

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Luffin-a, a ribosome-inactivating protein from the seeds of sponge gourd (Luffa cylindrica), was modified with 2,4,6-trinitrobenzenesulfonic acid (TNBS) at pH 8.0 and 20 degrees C. The inhibitory activity of the modified luffin-a on protein synthesis using rabbit reticulocyte lysate was lost rapidly

Cloning and Expression of Luffin-b cDNA from the Seeds of Luffa cylindrica.

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Luffin-b with Mr. 28 kD, isolated from the seeds of Luffa cylindrica,is one of the most toxic single chain plant ribosome inactivating proteins. The cDNA sequence of luffin-b was already reported by Kataoka in 1992. In this work, the luffin-b gene(lufB) coding sequence was cloned from the fresh

Cloning and soluble expression of mature alpha-luffin from Luffa cylindrica and its antitumor activities in vitro.

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Luffin-a, a single-chain Type I ribosome-inactivating protein, which is known to be the most toxic of the luffin family and apparently possesses antitumor activity, was isolated from Luffa cylindrica seeds. In the present study, mature alpha-luffin was cloned from L. cylindrica and it was found that

Purification and characterization of Luffin P1, a ribosome-inactivating peptide from the seeds of Luffa cylindrica.

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A peptide designated Luffin P1 was purified from the seeds of Luffa cylindrica. Its molecular mass was determined to be 5226.1 Da by MALDI-TOF MS analysis. The purified Luffin P1 shows a strong inhibitory activity on protein synthesis in the cell-free rabbit reticulocyte lysate with IC(50) of 0.88

Structural characterization and anti-HIV-1 activities of arginine/glutamate-rich polypeptide Luffin P1 from the seeds of sponge gourd (Luffa cylindrica).

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Luffin P1, the smallest ribosome-inactivating peptide from the seeds of Luffa cylindrica was found to have anti-HIV-1 activity in HIV-1 infected C8166 T-cell lines and be able to bind with HIV Rev Response Element. Nuclear magnetic resonance spectroscopy revealed that the Luffin P1 comprises a

Complete amino acid sequence of luffin-b, a ribosome-inactivating protein from sponge gourd (Luffa cylindrica) seeds.

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The complete amino acid sequence of luffin-b has been determined. All the twenty-seven tryptic peptides were isolated by reverse-phase HPLC from the tryptic digests of intact luffin-b and one of its CNBr fragments (CB4), and sequenced using the DABITC/PITC double coupling method. The overlap of

Complete amino acid sequence of luffin-a, a ribosome-inactivating protein from the seeds of sponge gourd (Luffa cylindrica).

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The complete amino acid sequence of luffin-a has been determined. Twenty-two peptides were isolated from the tryptic digest of luffin-a and sequenced employing the DABITC/PITC double coupling method. Overlaping of these peptides was achieved by analyzing the chymotryptic peptides or CNBr-fragments

Isolation, Purification and Characterization of a Group of Novel Small Molecular Ribosome Inactivating Protein -- LuffinS from Seeds of Luffa cylindrica.

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A group of novel RIPs--LuffinS(1), LuffinS(2), LuffinS(3) (MW about 8 kD) were purified by ammonia sulfate precipitation, CM-52 chromatography, HRLC size chromatography and Mono S FPLC. LuffinS(1), LuffinS(2) and LuffinS(3) have similar weight of about 8kD, and their N-terminal amino acid is Ala,

Chemical modifications of momordin-a and luffin-a, ribosome-inactivating proteins from the seeds of Momordica charantia and Luffa cylindrica: involvement of His140, Tyr165, and Lys231 in the protein-synthesis inhibitory activity.

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Effects of chemical modifications on the protein-synthesis inhibitory (PSI) activities of momordin-a and luffin-a were investigated. Treatment with a 50-fold excess of diethylpyrocarbonate at pH 6.5 modified one histidine residue in momordin-a and luffin-a and reduced their PSI activities to 10% and

Nucleotide sequence of cDNA encoding alpha-luffin, a ribosome-inactivating protein from Luffa cylindrica.

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Nucleotide sequence of cDNA encoding beta-luffin, another ribosome-inactivating protein from Luffa cylindrica.

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Complete amino acid sequence of luffin-a, a ribosome-inactivating protein from the seeds of Luffa cylindrica.

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Cloning and soluble expression of mature α-luffin from Luffa cylindrica in E. coli using SUMO fusion protein.

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α-Lufin, found in Luaf cylindrica seeds, is a type I ribosome inactivating proteins. Cytotoxic effects make it an appropriate candidate for the construction of immunotoxins and conjugates. Because of limited natural resources, recombinant technology is the best approach to achieve large-scale

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