Abstract
A ribosome inactivating peptide, with an N-terminal sequence exhibiting pronounced similarity to that of the 6.5 kDa-arginine/glutamate-rich polypeptide from Luffa cylindrica seeds, was isolated from seeds of a closely related species, the ridge gourd Luffa acutangula. The 5.6 kDa-peptide designated luffangulin inhibited cell-free translation with an IC50 of 3.5 nM but lacked inhibitory activity toward HIV-1 reverse transcriptase. It was similar to luffaculin, the 28 kDa ribosome inactivating protein in being unadsorbed on DEAE-cellulose and adsorbed on Affi-gel blue gel. On CM-cellulose luffangulin and luffaculin appeared as two adjacent peaks.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amidohydrolases / metabolism
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Amino Acid Sequence
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Animals
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Antiviral Agents / pharmacology
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Chromatography, High Pressure Liquid
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Electrophoresis, Polyacrylamide Gel
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Glycoproteins / isolation & purification*
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Glycoproteins / pharmacology
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HIV Reverse Transcriptase / antagonists & inhibitors
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HIV Reverse Transcriptase / metabolism
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Humans
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Inhibitory Concentration 50
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Luffa / chemistry*
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Molecular Sequence Data
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Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase
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Plant Proteins / isolation & purification*
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Plant Proteins / pharmacology
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Rabbits
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Reticulocytes / metabolism
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Ribosome Inactivating Proteins, Type 1
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Ribosomes / drug effects*
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Seeds / chemistry*
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Sequence Homology, Amino Acid
Substances
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Antiviral Agents
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Glycoproteins
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LRIP-I protein, Luffa cylindrica
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Plant Proteins
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Ribosome Inactivating Proteins, Type 1
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luffaculin protein, Luffa acutangula
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HIV Reverse Transcriptase
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Amidohydrolases
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Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase