[The purification and characterization of a novel lipid transfer protein from caryopsis of barnyard grass (Echinochloa crusgalli)].

A novel lipid transfer protein called Ec-LTP was isolated from resting caryopsis of weed barnyard grass Echinochloa crusgalli (L.) Beauv.; its molecular weight, amino acid content and N-terminal amino acid sequence were determined.

[Isolation of the lipid-transporting protein Ns-LTP1 from seeds of the garden fennel flower (Nigella sativa)].

A novel lipid-transporting protein (Ns-LTP1) has been isolated from seeds of the garden fennel flower Nigella sativa. The molecular mass, N-terminal amino acid sequence, and amino acid composition of the protein have been determined. Ns-LTP1 has a molecular mass of 9602 Da and contains eight cysteine residues which form four disulfide bridges.

[Identification of the N-terminal peptide of bovine tryptophanyl-tRNA-synthetase].

By means of covalent chromatography on thiopropyl-sepharose 6B the N-terminal, as well as other tryptic cysteine-containing peptides of the bovine tryptophanyl-tRNA-synthetase (EC 6.1.1.

Primary structure of three cationic peptides from porcine neutrophils. Sequence determination by the combined usage of electrospray ionization mass spectrometry and Edman degradation.

The primary structure of three major cationic peptides from porcine neutrophils has been determined. The sequencing was made by the combined use of electrospray ionization mass spectrometry and Edman degradation. The determined sequences unambiguously show that these peptides can not be considered as defensins.