Histochemical and Thin Layer Chromatographic Analyses of Neutral Lipids in Echinostoma revolutum Metacercariae Cultured In vitro

1977 ◽  
Vol 63 (6) ◽  
pp. 1041 ◽  
Author(s):  
Mark S. Butler ◽  
Bernard Fried
Keyword(s):  
Thin Layer ◽  
Neutral Lipids ◽  
Echinostoma Revolutum

Pairing and aggregation of Amblosoma suwaense (Trematoda: Brachylaimidae) metacercariae in vitro and partial characterization of lipids involved in chemo-attraction

Parasitology ◽  
1981 ◽  
Vol 82 (2) ◽  
pp. 225-229 ◽  
Author(s):  
B. Fried ◽  
G. A. Robinson
Keyword(s):  
Thin Layer ◽  
Neutral Lipid ◽  
Sterol Ester ◽  
Neutral Lipids ◽  
Sterol Esters ◽  
Free Sterols ◽  
Lipid Fractions ◽  
Oil Red O

SUMMARYHistochemical and thin-layer chromatographic (t.l.c.) analyses were made on neutral lipids in the free (unencysted) metacercariae of Amblosoma suwaense (Brachylaimidae). As determined by t.l.c. the major neutral lipid fractions in metacercariae removed directly from Campeloma decisum snails were free sterols and sterol esters. Metacercariae incubated for 1 h at 37±1° C in sterile Locke's solution released mainly sterol esters and a lesser amount of free sterols into the medium. As determined by Oil Red O (ORO) staining, metacercariae accumulated neutral lipid in the intestinal caeca during incubation and the excretory system was ORO negative. Behavioural studies showed that metacereariae paired and aggregated in vitro and were attracted to lipophilic but not to hydrophilic worm products. Following t.l.c. preparative analysis it was demonstrated that metacercariae were attracted to sterol ester worm products but not to free sterol products.

Intraspecific and interspecific pairing of Haematoloechus medioplexus (Trematoda) and Echinostoma revolutum (Trematoda) adults in vitro, and observations on H. medioplexus lipophilic excretory–secretory products

Parasitology ◽  
1982 ◽  
Vol 84 (2) ◽  
pp. 375-380 ◽  
Author(s):  
B. Fried ◽  
D. A. Leiby
Keyword(s):  
Fatty Acids ◽  
Thin Layer ◽  
Chromatographic Analysis ◽  
Petri Dish ◽  
Temperature Tolerance ◽  
Echinostoma Revolutum ◽  
Agar Substrate ◽  
Secretory Products ◽  
Thin Layer Chromatographic Analysis

SUMMARYIntraspecific pairing of Haematoloechus medioplexus and Echinostoma revolutum adults and interspecific pairing of H. medioplexus and E. revoltum adults were studied in vitro at 21 ± 1 °C and 30 ± 1 °C in Petri-dish cultures containing an agar substrate and a Locke's 1:1 solution overlay. Salinity and temperature tolerance tests showed that both species survived for 24 h in a Locke's 1:1 solution at 21 ± 1 °C and 30 ±1 °C. For behaviour studies, worms were placed 2 cm apart and then observed at various intervals from 5 min to 4 h. H. medioplexus and E. revolutum showed significant intraspecific pairing at 30±1 °C, whereas only H. medioplexus paired significantly at 21±1°C. Significant interspecific pairing of H. medioplexus and E. revolutum occurred at 21 ±1 °C and 30 ±1 °C. Thin-layer chromatographic analysis showed that H. medioplexus adults released mainly free sterol, along with traces of triacylglycerols and free fatty acids into a non-nutrient medium.

Phytochemical, Analytical and Medicinal Studies of Holoptelea integrifolia Roxb. Planch - A Review

2019 ◽  
Vol 5 (4) ◽  
pp. 270-277 ◽  
Author(s):  
Vijay Kumar ◽  
Simranjeet Singh ◽  
Ragini Bhadouria ◽  
Ravindra Singh ◽  
Om Prakash
Keyword(s):  
Liquid Chromatography ◽  
Thin Layer ◽  
Thin Layer Chromatography ◽  
High Performance ◽  
Biologically Active ◽  
Toxicological Studies ◽  
Wide Range ◽  
Layer Chromatography

Holoptelea integrifolia Roxb. Planch (HI) has been used to treat various ailments including obesity, osteoarthritis, arthritis, inflammation, anemia, diabetes etc. To review the major phytochemicals and medicinal properties of HI, exhaustive bibliographic research was designed by means of various scientific search engines and databases. Only 12 phytochemicals have been reported including biologically active compounds like betulin, betulinic acid, epifriedlin, octacosanol, Friedlin, Holoptelin-A and Holoptelin-B. Analytical methods including the Thin Layer Chromatography (TLC), High-Performance Thin Layer Chromatography (HPTLC), High-Performance Liquid Chromatography (HPLC) and Liquid Chromatography With Mass Spectral (LC-MS) analysis have been used to analyze the HI. From medicinal potency point of view, these phytochemicals have a wide range of pharmacological activities such as antioxidant, antibacterial, anti-inflammatory, and anti-tumor. In the current review, it has been noticed that the mechanism of action of HI with biomolecules has not been fully explored. Pharmacology and toxicological studies are very few. This seems a huge literature gap to be fulfilled through the detailed in-vivo and in-vitro studies.

scholarly journals Studies on the autophosphorylation of the insulin receptor from human placenta. Analysis of the sites phosphorylated by two-dimensional peptide mapping

1988 ◽  
Vol 252 (2) ◽  
pp. 607-615 ◽  
Author(s):  
J M Tavaré ◽  
R M Denton
Keyword(s):  
Thin Layer ◽  
Insulin Receptor ◽  
Peptide Mapping ◽  
Beta Subunit ◽  
Two Dimensional ◽  
Intact Cells ◽  
Tyrosine Residues ◽  
Domain 3 ◽  
Receptor Beta

1. A partially purified preparation of human placental insulin receptors was incubated with [gamma-32P]ATP in the presence or absence of insulin. The 32P-labelled insulin-receptor beta-subunits were then isolated, cleaved with trypsin followed by protease V8 and the [32P]phosphopeptides generated were analysed by thin layer electrophoresis and chromatography. This approach revealed that insulin stimulates autophosphorylation of the insulin-receptor beta-subunit in vitro on at least seven tyrosine residues distributed among three distinct domains. 2. One domain (domain 2), containing tyrosine residues 1146, 1150 and 1151 was the most rapidly phosphorylated and could be recovered as mono-, di- and triphosphorylated peptides cleaved by trypsin at Arg-1143 and either Lys-1153 or Lys-1156. Multiple phosphorylation of this domain appears to partially inhibit the cleavage at Lys-1153 by trypsin. 3. In a second domain (domain 3) containing two phosphorylated tyrosine residues at positions 1316 and 1322 the tyrosines were phosphorylated more slowly than those in domain 2. This domain is close to the C-terminus of the beta-subunit polypeptide chain. 4. At least two further tyrosine residues appeared to be phosphorylated after those in domains 2 and 3. These residues probably residue within a domain lying in close proximity to the inner face of the plasma membrane containing tyrosines 953, 960 and 972, but conclusive evidence is still required. 5. The two-dimensional thin-layer analysis employed in this study to investigate insulin-receptor phosphorylation has several advantages over previous methods based on reverse-phase chromatography. It allows greater resolution of 32P-labelled tryptic peptides and, when coupled to radioautography, is considerably more sensitive. The approach can be readily adapted to study phosphorylation of the insulin receptor within intact cells.

Thin-Layer Chromatographic Analysis of Phospholipids in Echinostoma revolutum (Trematoda) Adults

1979 ◽  
Vol 65 (2) ◽  
pp. 243 ◽  
Author(s):  
Bernard Fried ◽  
Irwin L. Shapiro
Keyword(s):  
Thin Layer ◽  
Chromatographic Analysis ◽  
Echinostoma Revolutum ◽  
Thin Layer Chromatographic Analysis

Thin layer chromatographic analyses of amino acids in Echinostoma revolutum (Trematoda) adults

1977 ◽  
Vol 7 (6) ◽  
pp. 497-499 ◽  
Author(s):  
Robert S. Bailey ◽  
Bernard Fried
Keyword(s):  
Amino Acids ◽  
Thin Layer ◽  
Echinostoma Revolutum
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