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

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

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 these peptides was achieved by analyzing the CNBr fragments and their chymotryptic peptides. Luffin-b...

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Amino acid sequences of the two smallest trypsin inhibitors from sponge gourd seeds.

Sponge gourd (Luffa cylindricd) seeds contain several biologically active proteins. Recently, we found that the mature seeds contain three types of trypsin inhibitors having molecular masses of about 13 kDa (type I), 6.5 kDa (type II), and 3.2 kDa (type III). Furthermore, preliminary experiments suggested that the type III one might be a domain unit of these inhibitors. Here, we present the iso...

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Pretreating Luffa Sponge (Luffa cylindrica L.) with Concentrated Phosphoric Acid and Subsequent Enzymatic Saccharification

Luffa was evaluated as a potential energy crop. A considerable amount of luffa sponge biomass can be grown in a vertical direction with approximately 70% polysaccharide content and low lignin content. When concentrated H3PO4 was employed to pretreat luffa sponge, hemicelluloses were the most sensitive component, followed by cellulose and lignin. Hemicellulose solubilization and cellulose loss p...

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Isolation and partial characterization of three protein-synthesis inhibitory proteins from the seeds of Luffa cylindrica.

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) have molecular masses of 19 kDa, 15 kDa, and 9 kDa, and were designated 19K-PSI, 15K-PSI, and 9K-PSI...

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Optimization of EnBase Fed-Batch Cultivation to Improve Soluble Fraction Ratio of α-Luffin Ribosome Inactivating Protein

Background: The increase of the protein expression via ribosomal manipulation is one of the suggested cellular mechanisms involved in EnBase fed-batch mode of cultivation. However, this system has not been implemented for cytotoxic proteins.Objectives: Here, the expression pattern of α-Luffin, a ribosome inactivation protein (RIP) with an innate toxicity,...

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ژورنال

عنوان ژورنال: Agricultural and Biological Chemistry

سال: 1990

ISSN: 0002-1369,1881-1280

DOI: 10.1271/bbb1961.54.2967