[The possibility of detecting soluble HLA antigens in traces of blood and excretions].

A modified lymphocytolysis inhibition test revealed that specific results may be attained in 50-60% of examinations of blood, spermatic, and salivary spots if highly specific HLA sera are used. HLA antigens were found to be present in spermatic and salivary spots for a year (follow-up period). Recommendations were developed for practical use of HLA antigens in examinations of blood, spermatic, and salivary spots by lymphocytolysis inhibition test in forensic medical expert evaluation.

[Study of the electrophoretic and kinetic properties of erythrocyte glucose-6-phosphate dehydrogenase in hereditary enzyme deficiencies. Description of a new variant of glucose-6-phosphate dehydrogenase: the Gd Kremenchug].

A study of the activity of human erythrocyte G-6-PD has been completed on a great number of normal controls, coming from different regions of the USSR. This study has led to the discovery of a new variant of erythrocytic Gd, which was named "Kremenchug" from the origin of the patient. This new Gd, has a very low Km for G-6-P, and has a greater affinity for 2-deoxyglucose-6-phosphate.

[Electrophoretic and kinetic properties of erythrocyte glucose-6-phosphate dehydrogenase (Gd) in hereditary enzyme deficiency. A new variant of glucose-6-phosphate dehydrogenase : Gd Kremenchug].

A study of the activity of human erythrocyte G-6-PD has been completed on a great number of normal controls, coming from different regions of the USSR. This study has led to the discovery of a new variant of erythrocytic Gd, which was named "Kremenchug" from the origin of the patient. This new Gd, has a very low Km for G-6-P, and has a greater affinity for 2-deoxyglucose-6-phosphate.

[Detection of a new anomalous variant of glucose-6-phosphate dehydrogenase in human erythrocytes].

Kinetic and electrophoretic properties of 230--300 fold purified preparations of glucose-6-phosphate dehydrogenase (G6PD) from red cells of donors and patients with acute drug hemolytic anemia due to G6PD deficiency were studied. A new abnormal variant of G6PD isolated from red cell of a patient with acute drug hemolytic anemia, which was not described in literature, has been discovered. The abnormal enzyme differs from the normal by decreased Michaelis constant for glucose-6-phosphate and nicotinamide adenine dinucleotide phosphate (NADP), by increased utilization of analogues of substrates--2-deoxy-glucose-6-phosphate and particularly deamino-NADP, by low thermal stability, by the character of pH-dependence, by the appearance of a single band of G6PD activity in polyacrylamide gel electrophoresis.