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Clinical analysis and evaluation of selected laboratory parameters in patients examined in distant periods after trichinellosis

100%

Pielok L.

Wiadomości Parazytologiczne

2001

tom 47

nr 2

Since early times, opinions of clinicians in distant sequele of the experienced once trichinellosis remain controversial. A set of studies was performed in 75 patients who had experienced trichinellosis 1, 3, 4, 6, or 7 years earlier. Persistence of the general clinical symptoms and of the motor system symptoms as well as persistence of IgG class antibodies against the E/S antigen of Trichinella sp. it was found in 77.3% examined patients. In 84.0% patients bioelectric disturbances (EMG, ENG) were detected. Parasitological studies and pathomorphological examination of muscle biopsies performed in 24 patients pointed to degradation of Trichinella larvae and to the incompletely extinguished pathological process.

Purification and characterization of alpha-amylases from the intestine and muscle of Ascaris suum [Nematoda]

100%

Zoltowska K.

Acta Biochimica Polonica

2001

tom 48

nr 3

α-Amylase (EC 3.2.1.1) was purified from the muscle and intestine of the parasitic helminth of pigs Ascaris suum. The enzymes from the two sources differed in their properties. Isoelectric focusing revealed one form of α-amylase from muscles with pI of 5.0, and two forms of amylase from intestine with pI of 4.7 and 4.5. SDS/PAGE suggested a molecular mass of 83 kDa and 73 kDa for isoenzymes of a-amylases from intestine and 59 kDa for the muscle enzyme. α-Amylase from intestine showed maximum activity at pH 7.4, and the enzyme from muscle at pH 8.2. The muscle enzyme was more thermostabile than the intestinal α-amylase. Both the muscle and intestine amylase lost half of its activity after 15 min at 70°C and 50°C, respectively. The Km values were: for muscle amylase 0.22 ,ug/ml glycogen and 3.33 ,ug/ml starch, and for intestine amylase 1.77 ug/ml glycogen and 0.48 ug/ml starch. Both amylases were activated by Ca and inhibited by EDTA, iodoacetic acid, p-chloromercuribenzoate and the inhibitor of α-amylase from wheat. No significant differences were found between the properties of a-amylases from parasites and from their hosts.

Ograniczanie wyników

1 Acta Biochimica Polonica

1 Wiadomości Parazytologiczne

1 Pielok L.

1 Zoltowska K.

2 2001

Wyniki wyszukiwania

Clinical analysis and evaluation of selected laboratory parameters in patients examined in distant periods after trichinellosis

Purification and characterization of alpha-amylases from the intestine and muscle of Ascaris suum [Nematoda]