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

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概要

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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 of luffin-a and their S. aureus V8 protease peptides. Luffin-a consists of 248 amino acid residues and its relative molecular mass is calculated to be 27,021 Da, excluding the attached sugar chains reasoned to be present at each Asn residue of positions 28, 33, 77, 84, 206, and 227. A comparison with the sequence of ricin A-chain showed 33% sequence identity indicating that these proteins are homologous.

• 社団法人日本農芸化学会の論文
• 1990-11-23

著者

• FUNATSU Gunki

  Laboratory of Biochemistry, Faculty of Agriculture, Kyushu University

• Nishida H

  Kyushu Univ. Fukuoka

• Nishida Hiromi

  Laboratory Of Biochemistry And Protein Chemistry Engineering Faculty Of Agriculture Kyushu Universit

• Nishida Hiromi

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

• ISLAM M.

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

• Funatsu Gunki

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

• Islam M.

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

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