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The amino-acid sequence of the nonspecific lipid transfer protein from germinated castor bean endosperms

1986; Elsevier BV; Volume: 870; Issue: 2 Linguagem: Inglês

10.1016/0167-4838(86)90229-3

1878-1454

Kunio Takishima, Shinichiro Watanabe, Mitsuhiro Yamada, Gunji Mamiya,

Biochemical and Structural Characterization

The amino-acid sequence of the nonspecific lipid-transfer protein from germinated castor bean endosperms has been determined by automatic sequencing of Staphylococcus aureus proteinase and tryptic peptides. The protein has 92 residues and a molecular weight of 9313. The complete primary structure of this protein is: Val-Asp-Cys-Gly-Gln-Val-Asn-Ser-Ser-Leu10-Ala-Ser-Cys-Ile-Pro-Phe-Leu-Thr-Gly-Gly20-Val-Ala-Ser-Pro-Ser-Ala-Ser-Cys-Cys-Ala30-Gly-Val-Gln- Asn-Leu-Lys-Thr-Leu-Ala-Pro40-Thr-Ser-Ala-Asp-Arg-Arg-Ala-Ala-Cys-Glu50-Cys-Ile-Lys-Ala-Ala-Ala-Ala-Arg-Phe-Pro60-Thr-Ile-Lys-Gln-Asp-Ala- Ala-Ser-Ser-Leu70-Pro-Lys-Lys-Cys-Gly-Val-Asp-Ile-Asn-Ile80-Pro-Ile-Ser-Lys-Thr-Thr-Asn-Cys-Gln-Ala90-Ile-Asn. Sequence microheterogeneity was found at residues 42 and 50, suggesting the occurrence of two genes for this protein or the allelic variation of the same gene. 12 of 14 acidic and basic amino acids were located on the latter half of the sequence. The first 20 residues of this protein have a homology (45%) with the residues 2–21 of the lipid-transfer protein from spinach leaf.