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The effect of Propionibacterium granulosum, glucan and isoprinosine on the course of the infection of mice with Trichinella spiralis

100%

Golinska Z., Bany J., Szmigielski S., Petruczenko A.

Acta Parasitologica

1992

tom 37

nr 4

The effect of Propionibacterium granulosum, glucan and isoprinosine on the course of infection of B6C3F₁ mice with T. spiralis was studied. The worm burdens in the intestinal and muscle phases of the infection and the weight of spleens were determined. The intensity of the infection was reduced mainly in mice exposed to P. granulosum, most clearly after intraperitoneal injection on the day of infection; only slight increase in weight of spleens was found in these mice. On the contrary, after exposure of mice to P. acnes, the intensity of infection and the weight of spleens were increased. The effect of glucan was dose dependent. Low single dose caused a decrease in the number of intestinal and muscle forms of the parasite. Higher doses of glucan did not have any effect on the intensity of the infection. Various doses of isoprinosine did not affect the elimination of T. spiralis, and rather showed a tendency to increase the intensity of the infection.

Ultracentrifugation studies of the location of the site involved in the interaction of pig heart lactate dehydrogenase with acidic phospholipids at low pH. A comparison with the muscle form of the enzyme

80%

Terlecki G., Czapinska E., Hotowy K.

Cellular and Molecular Biology Letters

2007

tom 12

nr 3

Lactate dehydrogenase (LDH) from the pig heart interacts with liposomes made of acidic phospholipids most effectively at low pH, close to the isoelectric point of the protein (pH = 5.5). This binding is not observed at neutral pH or high ionic strength. LDH-liposome complex formation requires an absence of nicotinamide adenine dinucleotides and adenine nucleotides in the interaction environment. Their presence limits the interaction of LDH with liposomes in a concentration-dependent manner. This phenomenon is not observed for pig skeletal muscle LDH. The heart LDH-liposome complexes formed in the absence of nicotinamide adenine dinucleotides and adenine nucleotides are stable after the addition of these substances even in millimolar concentrations. The LDH substrates and studied nucleotides that inhibit the interaction of pig heart LDH with acidic liposomes can be ordered according to their effectiveness as follows: NADH > NAD > ATP = ADP > AMP > pyruvate. The phosphorylated form of NAD (NADP), nonadenine nucleotides (GTP, CTP, UTP) and lactate are ineffective. Chemically cross-linked pig heart LDH, with a tetrameric structure stable at low pH, behaves analogously to the unmodified enzyme, which excludes the participation of the interfacing parts of subunits in the interaction with acidic phospholipids. The presented results indicate that in lowered pH conditions, the NADH-cofactor binding site of pig heart LDH is strongly involved in the interaction of the enzyme with acidic phospholipids. The contribution of the ATP/ADP binding site to this process can also be considered. In the case of pig skeletal muscle LDH, neither the cofactor binding site nor the subunit interfacing areas seem to be involved in the interaction.

Ograniczanie wyników

1 Acta Parasitologica

1 Cellular and Molecular Biology Letters

1 Bany J.

1 Czapinska E.

1 Golinska Z.

1 Hotowy K.

1 Petruczenko A.

1 Szmigielski S.

1 Terlecki G.

1 2007

1 1992

Wyniki wyszukiwania

The effect of Propionibacterium granulosum, glucan and isoprinosine on the course of the infection of mice with Trichinella spiralis

Ultracentrifugation studies of the location of the site involved in the interaction of pig heart lactate dehydrogenase with acidic phospholipids at low pH. A comparison with the muscle form of the enzyme