[Immunochemical tests in the diagnosis of diseases of the male reproductive system]. / Immunokhimicheskie testy v diagnostike zabolevanii muzhskoi reproduktivnoi sistemy.

Immunochemical tests were employed to measure proteins (acid phosphatase, prostatic beta-globulin, endometrial alpha-2-globulin, lactoferrin, carcinoembryonal antigen) in spermatic plasma and prostatic fluid from healthy subjects and patients with prostatic adenoma, cancer, chronic inflammation, defects of spermatogenesis. It was found that the overall concentration of acid phosphatase and prostatic beta-globulin may serve a diagnostic criteria to differentiate prostatic adenoma from cancer as in 93% of prostatic cancer this parameter did not exceed 400 micrograms/ml whereas in 75% of adenomas it was above 1200 micrograms/ml. Activity of chronic prostatitis can be assessed from lactoferrin test. The level of the organ-specific antigens (acid phosphatase and prostatic beta-globulin) and lactoferrin correlated with the severity of spermatogenesis disorders.

[Immunochemical tests for the risk of inflammatory diseases]. / Immunokhimicheskie testy riska vospalitel'nykh zabolevanii.

Immunochemical measurements of the blood serum acute-phase proteins (APP)--C-reactive, pregnancy-related alpha 2-glycoprotein, lactoferrin, immunoglobulins A, M, and G, carried out in 153 healthy men and 46 children, has revealed that an elevated level of at least one, and, more so, of two or three APP evidences the presence of an inflammatory process in the examinee. In a number of cases enhanced APP production correlated with a marked reduction of IgA and IgG concentrations. Measurements of APP may be employed as available laboratory screening markers of nonspecific latent inflammation in adults and children.

[Formation of interpolymer complexes with human seminal plasma proteins]. / Obrazovanie interpolimernykh kompleksov belkami semennoi plazmy cheloveka.

Formation of interpolymeric complexes was studied involving human lactoferrin, prostate beta-globulin, specific acid phosphatase and polymers of various nature: polysaccharides--heparin, dextran sulfate; polylysine-16; proteins--human albumin, equine hemoglobin, gelatin, protamine. Immunoelectrophoresis proved to be a sensitive procedure to register the interpolymeric complexes formed. Electrophoretic mobility of lactoferrin and prostatic beta-globulin was most distinctly altered. Mechanisms of the complexes formation, including ionic and hydrophobic interactions, are discussed.

[Immuno-chemical and physico-chemical properties of human prostatic beta-globulin]. / Immunokhimicheskie i fiziko-khimicheskie svoistva prostaticheskogo beta-globulina cheloveka.

Distribution of prostate beta-globulin in tissues was studied by means of rocket-linear immunoelectrophoresis. The concentration of protein, exceeding 0.1 microgram/ml, was detected only in prostate extracts, seminal plasma and prostatic fluid. Purification of human prostate beta-globulin and its main physico-chemical properties are described. The charge of the protein molecule was altered under influence of various factors. A minor carbohydrate component was detected in the prostate beta-globulin; the protein was found to interact noncovalently with heteropolysaccharides (heparin, dextran sulfate).

[Immunochemical and physico-chemical characteristics of lactoferrin in human body fluids]. / Immunokhimicheskaia i fiziko-khimicheskaia kharakteristiki laktoferrina biologicheskikh zhidkostei cheloveka.

It is proved that lactoferrins of different human body fluids (sperm, saliva, milk, tears, urine, bile, sweat, liquor, lymph, blood serum) are immunochemically identical. The lactoferrin is purified from milk, saliva and sperm and the identity of physical and chemical properties of lactoferrins of various origins is proved. The quantitative estimation of the contents of this protein in normal body fluids is given. It is detected the dependence of this protein' electrophoretic mobility and isoelectric point of degree of iron saturation. It is found that lactoferrin is capable to form complexes with esterase.