Ascaris suum, an Intestinal Parasite, Produces Morphine
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چکیده
منابع مشابه
Ascaris suum, an intestinal parasite, produces morphine.
The parasitic worm Ascaris suum contains the opiate alkaloid morphine as determined by HPLC coupled to electrochemical detection and by gas chromatography/mass spectrometry. The level of this material is 1168 +/- 278 ng/g worm wet weight. Furthermore, Ascaris maintained for 5 days contained a significant amount of morphine, as did their medium, demonstrating their ability to synthesize the opia...
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The Ascaris suum intestinal basement membrane was solubilized on reduction with P-mercaptoethanol in 1% sodium dodecyl sulfate and 1% sodium dodecyl sulfate, 8 M urea to the extent of 90% and lOO%, respectively. The reduced membrane consists of at least 17 polypeptides ranging in molecular weight from 22,500 to greater than 400,000, as determined by sodium dodecyl sulfate-polyacrylamide gel ele...
متن کاملAscaris suum
The nucleotide sequences of the mitochondrial DNA (mtDNA) molecules of two nematodes, Caenorhabditis elegans [13,794 nucleotide pairs (ntp)], and Ascaris suum (14,284 ntp) are presented and compared. Each molecule contains the genes for two ribosomal RNAs (+rRNA and 1-rRNA), 22 transfer RNAs (tRNAs) and 12 proteins, all of which are transcribed in the same direction. The protein genes are the s...
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The nematode intestine is a tissue of interest for developing new methods of therapy and control of parasitic nematodes. However, biological details of intestinal cell functions remain obscure, as do the proteins and molecular functions located on the apical intestinal membrane (AIM), and within the intestinal lumen (IL) of nematodes. Accordingly, methods were developed to gain a comprehensive ...
متن کاملComparative purification and characterization of invertebrate muscle glycogen synthase from the porcine parasite Ascaris suum.
Glycogen synthase has been purified from the obliquely striated muscle of the swine parasite Ascaris suum. The muscle contains a concentration of glycogen synthase and glycogen which is 20-fold and 15-fold, respectively, greater than rabbit skeletal muscle. The enzyme could not be solubilized with salivary amylase, but partial solubilization was achieved by activation of endogenous phosphorylas...
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ژورنال
عنوان ژورنال: The Journal of Immunology
سال: 2000
ISSN: 0022-1767,1550-6606
DOI: 10.4049/jimmunol.165.1.339