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luffin a/zuckermelone
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12 Ergebnisse
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
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
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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Complete amino acid sequence of luffin-a, a ribosome-inactivating protein from the seeds of Luffa cylindrica.
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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
Isolation and partial characterization of three protein-synthesis inhibitory proteins from the seeds of Luffa cylindrica.
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Three new proteins which inhibit protein synthesis in rabbit reticulocyte lysates were isolated from an extract of sponge gourd (Luffa cylindrica) seeds by chromatography on a AF-Blue Toyopearl column followed by FPLC with a Mono S column. These three protein-synthesis inhibitory proteins (PSIs)
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
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
N-acetyl-D-glucosamine-asparagine structure in ribosome-inactivating proteins from the seeds of Luffa cylindrica and Phytolacca americana.
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Glycosylation-site-containing peptides were isolated from the proteolytic digests of luffin-a, luffin-b, PAP-S and CNBr-fragments of PAP-S by reverse-phase HPLC, and their amino acid compositions and sequences were analyzed. Six peptides were obtained from luffin-a, and three each from luffin-b and
Balsamin, a novel ribosome-inactivating protein from the seeds of Balsam apple Momordica balsamina.
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Plant seeds, a rich source of proteins, are considered important for their application as functional ingredients in a food system. A novel ribosome-inactivating protein (RIP), balsamin was purified from the seeds of Balsam apple, Momordica balsamina. Balsamin was purified by ion exchange
Proteins with abortifacient, ribosome inactivating, immunomodulatory, antitumor and anti-AIDS activities from Cucurbitaceae plants.
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1. The biochemical characteristics and biological activities of eight Cucurbitaceae plant proteins designated trichosanthin (isolated from tubers of Trichosanthes kirilowii), beta-trichosanthin (isolated from tubers of Trichosanthes cucumeroides), alpha- and beta-momorcharins (isolated from seeds of
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