[Study of the three-dimensional structure of proteins by means of tritium labeling. II. Intramolecular distribution of tritium in the N-terminal part of myoglobin and the tertiary structure of protein].

The possible use of the method of 3H-label introduction by means of a 3H-atom beam for investigating the three-dimensional structure (surface) of proteins was studied. The intramolecular distribution of tritium in the N-terminal part of 3H-labelled sperm-whale myoglobin was studied. The results obtained are in good agreement with the X-ray analysis data on the polypeptide chain of the protein molecule.

[Comparative study of preparations of hirudin and "pseudohirudin"].

In contrast to hirudin, "pseudohirudin", which is practically devoid of the antithrombin activity, is represented as associates of di- and trimers. The molecular weight of the "pseudohirudin" monomer is by 2000 less than that for hirudin. This corresponds to the 20 amino acid residues difference calculated from the total number of the amino acid residues.

[Subtilisin 72: a serine protease from Bac. subtilis strain 72 - an enzyme similar to subtilisin Carlsberg].

Subtilisin 72, a serine proteinase secreted by Bac. subtilis strain 72 was purified by covalent chromatography on Sepharose sorbent containing p-(omega-aminomethyl)phenylboronic acid as a ligand. The homogeneity of subtilisin 72 was confirmed by isoelectrofocusing in a thin layer of polyacrylamide gel (pl 8.

Structural studies on glyceraldehyde-phosphate dehydrogenase from rat skeletal muscle.

The NH2-terminal amino acid sequence of rat skeletal muscle glyceraldehydephosphate dehydrogenase (D-glyceraldehyde-3-phosphate : NAD+ oxidoreductase(physphorylating), EC 1.2.1.

[Limited proteolysis of bovine pepsin].

A limited proteolysis of bovine pepsin (EC 3.4.4.