Non-Catalytic Detoxication of Acetylcholinesterase Inhibitors by Liver and Plasma Proteins

1989 ◽  
pp. 245-251
Author(s):  
Howard W. Chambers ◽  
Janice E. Chambers
Keyword(s):  
Plasma Proteins ◽  
Acetylcholinesterase Inhibitors

Immunoenzymatic demonstration of the simultaneous presence of transferrin, hemopexin and albumin in a same hepatocyte and their ultrastructural localization

1978 ◽  
Vol 36 (2) ◽  
pp. 88-89
Author(s):  
M. Kraemer ◽  
J. Foucrier ◽  
J. Vassy ◽  
M.T. Chalumeau
Keyword(s):  
Plasma Proteins ◽  
Rat Hepatocytes ◽  
Ultrastructural Localization ◽  
Carrier Proteins ◽  
Normal Cells ◽  
Adult Rat ◽  
Adult Rat Hepatocytes ◽  
Monospecific Antisera ◽  
Different Levels

Some authors using immunofluorescent techniques had already suggested that some hepatocytes are able to synthetize several plasma proteins. In vitro studies on normal cells or on cells issued of murine hepatomas raise the same conclusion. These works could be indications of an hepatocyte functionnal non-specialization, meanwhile the authors never give direct topographic proofs suitable with this hypothesis.The use of immunoenzymatic techniques after obtention of monospecific antisera had seemed to us useful to bring forward a better knowledge of this problem. We have studied three carrier proteins (transferrin = Tf, hemopexin = Hx, albumin = Alb) operating at different levels in iron metabolism by demonstrating and localizing the adult rat hepatocytes involved in their synthesis.Immunological, histological and ultrastructural methods have been described in a previous work.

Root cultures of Canscora decussata as a potential source of acetylcholinesterase inhibitors

Planta Medica ◽  
2015 ◽  
Vol 81 (16) ◽  
Author(s):  
NK Gaikwad ◽  
P Singh Bhadoria ◽  
A Mitra
Keyword(s):  
Acetylcholinesterase Inhibitors ◽  
Root Cultures ◽  
Potential Source

Isolation and characterization of acetylcholinesterase inhibitors from Piper longum Linn.

Planta Medica ◽  
2016 ◽  
Vol 81 (S 01) ◽  
pp. S1-S381
Author(s):  
Z Khatami ◽  
P Sarkheil ◽  
HR Adhami
Keyword(s):  
Acetylcholinesterase Inhibitors ◽  
Piper Longum ◽  
Isolation And Characterization

Investigation of the Free and Total Thyroxine-binding Capacity of Plasma Proteins in Thyroid Disorders

1971 ◽  
Vol 10 (04) ◽  
pp. 299-304
Author(s):  
József Takó ◽  
János Fischer ◽  
Jusztina Juhász ◽  
Ilona Sztraka ◽  
István Kapus ◽  
...  
Keyword(s):  
Blood Cell ◽  
Thyroid Function ◽  
Oral Contraceptives ◽  
Red Blood Cell ◽  
Plasma Proteins ◽  
Binding Capacity ◽  
Thyroid Disorders ◽  
Thyroid Function Tests ◽  
Total Thyroxine

SummaryThe results of thyroid function tests have been compared with data on the thyroxine-binding capacity of plasma proteins in hyper-, hypo- and euthyroid cases, the latter including women taking oral contraceptives (Infecundin). It was found that there exists a significant correlation of exponential nature between the in vitro red blood cell 125I-triiodothyronine uptake (RCU) and the free thyroxine-binding capacity of the thyroxine-inding globulin (TBG).

Patterns of Incorporation of 75Se-Methionine into Fibrinogen and Other Plasma Proteins in Rabbits Stimulated by Different Test Conditions

1973 ◽  
Vol 29 (01) ◽  
pp. 076-086 ◽  
Author(s):  
Uri Seligsohn ◽  
Samuel I. Rapaport ◽  
Ariella Zivelin
Keyword(s):  
Growth Hormone ◽  
Plasma Proteins ◽  
Tissue Injury ◽  
Injury Pattern ◽  
Experimental Conditions ◽  
Test Conditions

SummaryRabbits were injected with 75Se-Methionine (75SeM) 4-8 hr after being subjected to a variety of experimental conditions: injection of ACTH, growth hormone, glucagon, adrenalin, endotoxin, turpentine, hydrocortisone and laparotomy. All of these experimental conditions except injection of glucagon were associated with increased incorporation of 75SeM into fibrinogen. Three patterns of incorporation of 75SeM into plasma proteins were recognized: 1. the pituitary pattern, which was observed in animals injected with ACTH, growth hormone or endotoxin, and which was characterized by increased incorporation of 75SeM only into fibrinogen and by a delayed incorporation of 75SeM into α2 and β1 globulins; 2. the tissue injury pattern, which was characterized by a markedly increased incorporation of 75SeM into fibrinogen and no alteration in incorporation of 75SeM into α2 or β1 globulins; and 3. the pharmacologic corticosteroid pattern, which was characterized by a moderately increased incorporation of 75SeM into fibrinogen and a strikingly increased incorporation of 75SeM into α2 and β1 globulins.

Plasma Components which Interfere with Ristocetin-induced Platelet Aggregation

1975 ◽  
Vol 33 (03) ◽  
pp. 540-546 ◽  
Author(s):  
Robert F Baugh ◽  
James E Brown ◽  
Cecil Hougie
Keyword(s):  
Platelet Aggregation ◽  
Human Plasma ◽  
Plasma Proteins ◽  
Binding Protein ◽  
Plasma Heating ◽  
Protein S ◽  
Fold Increase ◽  
Normal Human Plasma ◽  
Preliminary Examination ◽  
Normal Human

SummaryNormal human plasma contains a component or components which interfere with ristocetin-induced platelet aggregation. Preliminary examination suggests a protein (or proteins) which binds ristocetin and competes more effectively for ristocetin than do the proteins involved in ristocetin-induced platelet aggregation. The presence of this protein in normal human plasma also prevents ristocetin-induced precipitation of plasma proteins at levels of ristocetin necessary to produce platelet aggregation (0.5–2.0 mg/ml). Serum contains an apparent two-fold increase of this component when compared with plasma. Heating serum at 56° for one hour results in an additional 2 to 4 fold increase. The presence of a ristocetin-binding protein in normal human plasma requires that this protein be saturated with ristocetin before ristocetin-induced platelet aggregation will occur. Variations in the ristocetin-binding protein(s) will cause apparent discrepancies in ristocetin-induced platelet aggregation in normal human plasmas.

Purification of the Antihemophilic Factor by Gel Filtration on Agarose

1969 ◽  
Vol 22 (03) ◽  
pp. 577-583 ◽  
Author(s):  
M.M.P Paulssen ◽  
A.C.M.G.B Wouterlood ◽  
H.L.M.A Scheffers
Keyword(s):  
Factor Viii ◽  
Plasma Proteins ◽  
Large Scale ◽  
Gel Filtration ◽  
Large Scale Preparation ◽  
Scale Preparation ◽  
Antihemophilic Factor

SummaryFactor VIII can be isolated from plasma proteins, including fibrinogen by chromatography on agarose. The best results were obtained with Sepharose 6B. Large scale preparation is also possible when cryoprecipitate is separated by chromatography. In most fractions containing factor VIII a turbidity is observed which may be due to the presence of chylomicrons.The purified factor VIII was active in vivo as well as in vitro.

Alterations in Vascular Endothelial Cell-related Plasma Proteins In Thalassaemic Patients and their Correlation with Clinical Symptoms

1995 ◽  
Vol 74 (04) ◽  
pp. 1045-1049 ◽  
Author(s):  
P Butthep ◽  
A Bunyaratvej ◽  
Y Funahara ◽  
H Kitaguchi ◽  
S Fucharoen ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Endothelial Cell ◽  
Immunosorbent Assay ◽  
Plasma Proteins ◽  
Clinical Symptoms ◽  
Vascular Endothelial Cells ◽  
Vascular Endothelial Cell ◽  
Enzyme Linked Immunosorbent Assay ◽  
Vascular Endothelial ◽  
Leg Ulcers

SummaryAn increased level of plasma thrombomodulin (TM) in α- and β- thalassaemia was demonstrated using an enzyme-linked immunosorbent assay (ELISA). Nonsplenectomized patients with β-thalassaemia/ haemoglobin E (BE) had higher levels of TM than splenectomized cases (BE-S). Patients with leg ulcers (BE-LU) were found to have the highest increase in TM level. Appearance of larger platelets in all types of thalassaemic blood was observed indicating an increase in the number of younger platelets. These data indicate that injury of vascular endothelial cells is present in thalassaemic patients.

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