Four free cysteine residues found in human IgG1 of healthy donors.

Modifications with different thiol reagents demonstrated that 28 of 32 cysteine residues of human IgG1 are involved in the formation of disulfide bonds, and four cysteines remain free. So IgG1 is a protein possessing both free SH-groups and disulfide bonds. Only one of the four SH-groups is accessible for silver or mercury ions and hydrophobic reagents, whereas the remaining three SH-groups are masked and can be revealed only after deep denaturation of the protein.

[Isolation and characterization of the ALP1 protease from Aspergillus fumigatus and its protein inhibitor from Physarium polycephalum].

It is known that Aspergillus fumigatus secretes a serine protease ALP1 of the subtilisin family in the presence of extracellular protein substrates. We found conditions of A. fumigatus culturing that provide a high ALP1 activity inside cells without induction by extracellular proteins.

[Determination of the accessible surface of lysozyme and human serum albumin molecules by the total tritium labeling method].

Amino acids composing an accessible surface of lysozyme and human serum albumin (HSA) globules were determined by the total tritium labelling method. A good correlation between our data on the distribution of the tritium label for the lysozyme molecule and X-ray data on the tertiary structure for this macromolecule was received. Lysozyme was used as a standard for determining the accessible surface of the globule albumin.

[The mechanism of binding of sodium dodecyl sulfate by lysozyme].

It has been shown that the mechanism of complex formation changes at variation of the detergent concentration. At low concentrations the complex is stabilized, mainly, by hydrophobic interactions. The boded molecules are immobilized inside the globules.