Results 211 to 220 of about 14,451 (254)
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Collection of Fertile Ascaris suum Eggs
The Journal of Parasitology, 1986does it seem to affect the pseudopodial activity of activated cells (results not shown). While sperm adenylate cyclase activity and cyclic AMP may not be required for Ascaris sperm activation, a chemotactic role cannot be excluded for exogenously produced cyclic-AMP during the sperm's migration in the female reproductive tract.
E L, Jeska, J P, Caruso, M J, Donahue
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Enzyme Polymorphism in Ascaris suum (Nematoda)
The Journal of Parasitology, 1982The potential of multilocus electrophoretic studies for providing insight into the population biology of parasitic organisms was studied using the swine parasite Ascaris suum suum. Thirty-eight loci encoding enzymatic or nonenzymatic proteins have been resolved in extracts of adult worms by starch-gel electrophoresis.
J F, Leslie +3 more
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Lysophospholipase Activation with Ascaris suum Extract
The Journal of Parasitology, 1984In vivo lysophospholipase activity in mammals with nematode infections has been shown to be associated with increased tissue eosinophilia (Larsh et al., 1974, Exp. Parasitol. 36: 299306) and with the activation of lymphocytes (Goven and Moore, 1980, Z. Parasitenkd. 61: 265-269).
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Trypsin modification of phosphofructokinase from Ascaris suum
Molecular and Biochemical Parasitology, 1991Phosphofructokinase from Ascaris suum is a tetramer with subunits of 90 kDa. Treatment of the native enzyme with trypsin (10%, w/w) followed by SDS-gel electrophoresis was shown to immediately generate a 40-kDa fragment followed by a gradual formation of two other fragments of 37 and 32 kDa.
P A, Ahanotu +3 more
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Accessory Nuclei in Female Ascaris suum
The Journal of Parasitology, 1981Accessory nuclei were observed in early meiotic prophase (leptotene) in female Ascaris suum but such structures were absent in meiosis in males. Accessory nuclei also were observed during the prediminution embryonic divisions. All embryos did not have accessory nuclei, thus, those embryos with these structures may be female since the accessory nuclei ...
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γ-Glutamyl transpeptidase activity in Ascaris suum
Molecular and Biochemical Parasitology, 1986Using histochemical techniques gamma-glutamyl transpeptidase activity has been localized mainly in the cuticle-hypodermis in Ascaris suum. The specific activity of gamma-glutamyl transpeptidase was 3.87 +/- 0.49 mumol h-1 (g tissue)-1 in cuticle-hypodermis as compared to gastrointestinal tract, where it was 0.07 +/- 0.02 mumol h-1 (g tissue)-1, and ...
P D, Dass, M J, Donahue
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Biosynthesis of biopterin in Ascaris lumbricoides suum
Biochimica et Biophysica Acta (BBA) - General Subjects, 1980In in vivo experiments, radioactivity from [U-14C]GTP was incorporated into biopterin, and, in fact, all carbon atoms of biopterin synthesized in Ascaris lumbricoides suum originated from GTP. Biopterin was also biosynthesized in homogenates of tissue fluid and muscles of Ascaris lumbricoides suum.
H, Otsuka, K, Sugiura, M, Goto
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Demonstration of cobamide coenzyme in Ascaris suum
Comparative Biochemistry and Physiology Part B: Comparative Biochemistry, 1975Abstract 1. 1. Cobamide coenzyme was extracted from the body wall of adult female Ascaris suum maintained in Ellison's medium containing vitamin B 12 . 2. 2. The identification of the coenzyme in purified fractions was based on (a) specific spectral changes following treatment of the preparation with light and cyanide, (b) coenzyme activity
H, Oya, P P, Weinstein
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The Secretory Activity of Ascaris suum Intestine
The Journal of Parasitology, 1974Large amounts of granules, interpreted as secretory in nature, are found in the terminal web region of intestinal cells of freshly collected Ascaris suum. Morphologically identical granules are scattered throughout the apical half of the cell cytoplasm and appear to be formed at the lateral ends of the Golgi saccules. Silver-proteinate-stained sections
M, Borgers, S, De Nollin
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Protein phosphotyrosine phosphatases in Ascaris suum muscle
Molecular and Biochemical Parasitology, 1996Two forms of protein tyrosine phosphatases were partially purified from the musculo-cutaneous layer of Ascaris suum. A 50-55-kDa soluble form of the phosphatase cross-reacted with antisera raised against human PTP-1B and TC-PTP. Like the enzyme of human origin the phosphatase from Ascaris exhibited a preference for anionic substrates (tyrosine ...
B, Schmid +4 more
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