Human Gene Expression Alters Active Zone Distribution and Spontaneous Neurotransmitter Release at the Larval Neuromuscular Junction.

This study provides further insight into the molecular mechanisms that control neurotransmitter release. Experiments were performed on larval neuromuscular junctions of transgenic lines with different levels of human amyloid precursor protein (APP) production. To express human genes in motor neurons of , the UAS-GAL4 system was used.

[Special role of phosphate in the stability of the protein to the destruction by polyelectrolyte].

X-ray analysis shows the presence of specific anion-binding sites in proteins for sulfate, citrate and phosphate ions, but the functional role of these anions is not always clear. Thus, it is unknown which of the two types, mono- or divalent phosphate, plays an important role in the stability of proteins to stress effects on cells. In the present work, the influence of phosphate, sulfate, and chloride salt on the stability of lactate dehydrogenase (LDH) to its destruction by poly(styrenesulphonate) (PSS) was investigated by the methods of steady-state kinetics and the own protein fluorescence.

[Interaction of protein with charged colloidal particles].

The functional state of three proteins of different molecular weight (urease, lactate dehydrogenase, and hemoglobin) in the presence of the linear polyelectrolytes poly(allylamine hydrochloride) (PAA) and sodium poly(styrenesulfonate) (PSS) in the dissolved state and of the same polyelectrolytes bound to the surface of microspheres has been investigated. Microspheres were prepared by consecutive absorption of oppositely charged polyelectrolytes so that the outer layer of the shell was PAA for the acidic protein urease, and PSS for the alkaline proteins LDH and hemoglobin. It was shown that the dissolved polyelectrolyte completely inactivates all three proteins within one minute with a slight difference in the time constant.

[Thermal stability of lactate dehydrogenase in the complex with the anion polyelectrolyte poly(styrene sulfonate)].

The temperature stability of the cytoplasmic enzyme of the glycolysis of lactate dehydrogenase from a pig muscle (isoenzyme M4) in a complex with the anion polyelectrolyte poly(styrenesulfonate) has been investigated by the methods of adiabatic differential scanning microcalorimetry, the own protein fluorescence, and circular dichroism. Calorimetric investigations of complex of lactate dehydrogenase with poly(styrenesulphonate) in 50 mM phosphate buffer at pH 7.0 have shown that the temperature of the transition and enthalpy of lactate dehydrogenase thermal denaturation sharply decreases with growing weight ratio poly(styrenesulphonate)/lactate dehydrogenase, though at 20 degrees C the enzyme activity of lactate dehydrogenase remains unchanged for several hours irrespective of the addition of poly(styrenesulphonate).

[Incapsulation of enzymes into polyelectrolyte nano- and microcapsules and the problem of the development of enzymatic microdiagnostics].

The incapsulation of proteins into polyelectrolyte microcapsules (PE-microcapsules) has been studied with the aim to develop microdiagnostica for the presence of low-molecular-weight compounds in native biological fluids. The problem was solved using two enzymes: lactate dehydrogenase and urease. Polyelectrolyte microcapsules were prepared using two polyanions: polystyrene sulfonate (PSS) and dextran sulfate (DS), and two polycations: polyallylamine (PAA) and polydiallylmethylammonium (PDADMA).