Results 291 to 300 of about 1,339,631 (349)
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Plasma protein binding of ceftriaxone

Xenobiotica, 1987
1. The plasma protein binding characteristics of ceftriaxone, a new cephalosporin antibiotic, were determined in human, baboon, rabbit, dog and rat plasma. 2. The protein binding of ceftriaxone was similar and concentration-dependent in human, baboon, rabbit and rat plasma, being highly bound (90-95%) at low concentrations (less than 100 micrograms/ml)
W G Crouthamel, I. Bekersky, A C Popick
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Plasma protein binding of carbamazepine

Clinical Pharmacology & Therapeutics, 1975
The binding of carbamazepine to the pro teins of human plasma has been studied using ultrafiltration techniques. In vitro studies at 37° C showed the relation between concentration of unbound drug and total drug to be linear thraugh the range of total concentration of 5 to 50 µg/ml.
Hooper W.D.   +6 more
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Plasma protein binding of norethisterone

Contraception, 1982
Norethisterone (NET) is transported in the blood stream bound to plasma proteins. It is generally believed that only the part of the hormone that is not bound to plasma proteins can exert biological activity. NET binds to albumin and, like other 19-nortestosterone derived progestins, it also binds to sex hormone binding globulin (SHBG).
Viveca Odlind   +2 more
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The binding of chlorothiazide to plasma proteins

Biochimica et Biophysica Acta (BBA) - Protein Structure, 1971
Abstract Association constants and values for the enthalpy and entropy of binding of chlorothiazide to human serum albumin have been determined by a variety of methods. The influence of chlorothiazide binding on the plasma levels of the hypotensive drug pempidine has been considered.
A. Rosen, A. Breckenridge
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THE BINDING OF URATE BY PLASMA PROTEINS

Australian Journal of Experimental Biology and Medical Science, 1979
SummaryProtein binding of urate may have some pertinence to the pathogenesis of goat. However, binding studies have been hampered by problems with in vitro methodology and by the problem of relating the results of in vitro studies to the physiological situation.In the present study urate binding was determined by an ultrafiltration procedure.
John Rl Masarei, Joseph Bertolini
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Plasma Protein Binding of Bepridil

The Journal of Clinical Pharmacology, 1985
The binding of the calcium‐channel blocking agent, bepridil HCl (Vascor), to plasma proteins was investigated using radiolabeled bepridil and equilibrium dialysis. Greater than 99.7% of added bepridil‐14C was found to freshly collected human plasma. The binding was characterized by a saturable high‐affinity site (KD = 32 ng/mL = 87 nM) on alpha1‐acid ...
Barry H. Dvorchik   +3 more
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Binding of flavonoids to plasma proteins

2001
International ...
Dangles, O.   +4 more
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The binding of ibuprofen to plasma proteins

European Journal of Clinical Pharmacology, 1983
The binding of ibuprofen to human serum albumin, normal plasma and plasma obtained from rheumatoid arthritic patients was studied using the method of ultracentrifugation. It was found that ibuprofen is more strongly bound to normal plasma than to human serum albumin although this result is probably explained by fatty acid contamination of the human ...
M Siddiqui, D M Grennan, Leon Aarons
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Lidocaine plasma protein binding

Clinical Pharmacology and Therapeutics, 1980
The percent of unbound lidocaine in the plasma of 24 healthy subjects was measured by equilibrium dialysis after addition of 3 microgram/ml C14 lidocaine hydrochloride. The percentage of unbound lidocaine varied from 19.9 to 38.8 (30.2 +/- 5, mean +/- SD) was inversely related to the concentration of alpha 1-acid glycoprotein (AAG) in the plasma (r ...
Barbara B. Kitchell   +4 more
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PLASMA RETINOL‐BINDING PROTEIN*

Annals of the New York Academy of Sciences, 1980
Vitamin A is mobilized from liver stores and transported in plasma in the form of the lipid alcohol retinol, bound to a specific transport protein, retinol-binding protein (RBP). A great deal is known about the chemical structure, metabolism, and biological roles of RBP. RBP is a single polypeptide chain with molecular weight close to 20,000.
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