N-Acetyl-D-glucosamine-Asparagine Structure in Ribosome-inactivating Proteins from the Seeds of Luffa cylindrica and Phytolacca americana

M. Rafiqul Islam, Sung Sil Kung, Yoshinobu Kimura, Gunki Funatsu

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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 PAP-S. All of these peptides were negative toward the phenol-H2SO4 reaction and gave only N-acetyl-D-glucosamine in gas chromatography after methanolysis and reacetylation. Amounts of N-acetyl-D-glucosamine in these peptides were determined as D-glucosamine to be approximately one mol per peptide by an amino acid analyzer after HC1 hydrolysis. Based on these results we concluded that Asn residues at positions of 28, 33, 77, 84, 206, and 227 in luffin-a, of 2, 78, and 85 in luffin-b, and of 10, 44, and 255 in PAP-S were glycosylated with only GlcNAc, and contained one residue per site.

Original languageEnglish
Pages (from-to)1375-1381
Number of pages7
JournalAgricultural and Biological Chemistry
Issue number5
Publication statusPublished - 1991


ASJC Scopus subject areas

  • Agricultural and Biological Sciences(all)
  • Biochemistry, Genetics and Molecular Biology(all)

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