Complete Amino Acid Sequence of Luffin-b, a Ribosome-Inactivating Protein from Sponge Gourd (Luffa cylindrica) Seeds(Biological Chemistry)

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概要

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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 these peptides was achieved by analyzing the CNBr fragments and their chymotryptic peptides. Luffin-b consists of 250 amino acid residues with a relative molecular mass of 27,275 Da. Investigation for glycosylation sites indicated that Asn at positions 2, 78, and 85 might carry sugars. Sequence comparison with luffin-a showed that amino acid substitution occured in 55 positions. Luffin-b contains three glycosylation sites instead of the six sites in luffin-a, of which two were found to be conserved.

• 社団法人日本農芸化学会の論文
• 1991-01-23

著者

• FUNATSU Gunki

  Laboratory of Biochemistry, Faculty of Agriculture, Kyushu University

• ISLAM M.

  Laboratory of Parasitic Diseases, National Institute of Animal Health, National Agricultural and Foo

• Funatsu Gunki

  Laboratory Of Protein Chemistry And Engineering Faculty Of Agriculture Kyushu University

• Funatsu Gunki

  Laboratory Of Biochemistry And ** Laboratory Of Protein Chemistry & Engineering Faculty Of Agric

• Hirayama Hiroshi

  Laboratory Of Protein Chemistry And Engineering Faculty Of Agriculture Kyushu University

• Islam M.

  Laboratory Of Protein Chemistry And Engineering Faculty Of Agriculture Kyushu University

• Islam M.

  Laboratory Of Biochemistry And ** Laboratory Of Protein Chemistry & Engineering Faculty Of Agric

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