[Primary structure of a short toxin from the venom of a vietnamese scorpion (Buthus sp.)]. / Pervichnaia struktura korotkogo toksina iz iada v'etnamskogo skorpiona Buthus sp.

The complete amino acid sequence of an important toxin (toxin 14) from the venom of a Vietnamese scorpion (Buthus occitanus sp.) has been determined, which includes 35 amino acid residues and three disulfide bridges (molecular weight, 3843 Da). The comparison of the sequence with sequences of short scorpion toxins led us to conclude that toxin 14 belongs to a novel group of toxins affecting the excitability of myelinated nerves.

[Amino acid sequence of anionic protease inhibitors from buckwheat seeds]. / Aminokislotnye posledovatel'nosti anionnykh ingibitorov proteaz iz semian grechikhi.

Complete amino acid sequence of IT1 protease inhibitor and partial amino acid sequences of IT2 and IT4 protease inhibitors from buckwheat Fagopyrum esculentum Moench seeds were determined by automatic Edman degradation and mass spectrometry. IT1 inhibitor comprises 69 amino acid residues and its molecular mass is 7743.8 D. N-terminal 48 amino acid residues of IT2 inhibitor are identical to similar sequence of IT1 inhibitor. The sequence of 10 amino acid residues of IT4 inhibitor is completely identical to a part of the sequence of IT1 inhibitor C-terminally adjacent to its active site. Analysis of amino acid sequences of IT1, IT2 and IT4 inhibitors suggests that the proteins are the members of the potato proteinase inhibitor 1 family and include Arg-Asp residues in their active site.

[Search for new products of gene expression in human cardiac muscle. Microsequencing of proteins after two-dimensional electrophoresis]. / Poisk novykh produktov gennoi ékspressii v serdechnoi myshtse cheloveka. Mikrosekvenirovanie belkov posle dvumernogo élektroforeza.

Proteins of the human heart muscle were studied using modified two-dimensional electrophoresis. After separation, proteins were electroblotted onto Immobilon P membranes and several protein spots were used for microsequencing analysis. In most cases the proteins analyzed have blocked N-terminal amino acids. In order to study the primary structure of these proteins, hydrolysis in situ by trypsin followed by reversed-phase HPLC and microsequencing of the resulting peptides were performed. Four protein were identified in 8 analyzed fractions, specifically myosin light chain 1 (MLCl-V/sB), fatty-acid binding protein (heart isoform), alpha (B)-crystallin and alpha-tropomyosin. Amino acid sequences of two proteins were not found among human amino acid sequences collected in SWISSPROT bank (v. 21).