[Comparative characteristics of antigenic immunosorbents for isolating antibodies to LDH5].

The authors compare the methods for immobilization of porcine lactate dehydrogenase-5 (LDH5) on various carriers to be used for the preparation of an effective immunosorbent for the isolation of monospecific antibodies. Covalent binding of the enzyme with the carrier via a spacer grouping with the use of glutaraldehyde is advisable for LDH M4-isoform that is characterized by a quaternary structure.

[Isolation and immunochemical properties of LDG-5 from swine muscle].

Homogeneous crystalline isoenzyme LDH5 was isolated from pig muscles with a yield of 33%. Antiserum, developed to the purified LDH5 preparation from pig muscles, reacted with human and pig LDH isoenzymes containing M subunits and did not interact with LDH1 isoenzyme. The heterologous antiserum might be used for estimation of LDH1 content in human blood serum.

[Preparation of a staphylococcal immunosorbent sensitized by antibodies to the M-subunit of LDH].

A simple and rapid immunochemical procedure is developed for estimation of the LDH1 activity which involved separation of LDH1 from other LDH isoenzymes using immunosorbent. The immunosorbent consisted of killed Staphylococcus aureus cells, membrane of which contained protein A with absorbed antibodies towards M-subunits of porcine LDH.

[Tryptic peptides of maleylated alpha-chain of histidine decarboxylase from Micrococcus sp. n].

The maleylated alpha-chain of histidine decarboxylase from Micrococcus sp. n., containing 10 arginine residues was hydrolyzed by trypsin, and 9 peptides were isolated from the tryptic hydrolysate.

[Dependence of pepsin conformational states on pH and temperature].

A conformational behaviour of pepsin depending on pH and temperature was studied by circular dichroism, differential UV-spectroscopy, calorimetry and enzymatic hydrolysis kinetics. A subtile conformational transition of the enzyme accompanied by changes in the physico-chemical and enzymatic properties of the protein was observed within the temperature interval of 15--40 degrees and within the pH range of 1,1--5,6. The range of pepsin heat denaturation was studied.