The Binding of Thiocyanate to Albumin

نویسنده

  • HERBERT SCHEINBERG
چکیده

Since the report of Crandall and Anderson (1) in 1934, the distribution of thiocyanate ion in the body has been used as a measure of extracellular fluid volume. All such work has been based on the procedure of administering a known amount of a thiocyanate, and after an interval, measuring the concentration of thiocyanate in the serum. The amount of thiocyanate injected, or more accurately, the thiocyanate remaining in the body at this time, is divided by the serum concentration, and the resulting number is termed the "thiocyanate space." The assumptions usually made, implicitly or explicitly, in this procedure are that thiocyanate is not metabolized and does not penetrate cells except red cells, that equilibrium exists between serum and extravascular thiocyanate, and that the thiocyanate concentration is essentially the same in the extravascular fluid as it is in the serum. The work reported in this paper' shows that the latter assumption is wrong and that the error resulting from its use is great. Methods of determining serum thiocyanate measure total thiocyanate since they depend on calibration curves made from known amounts of thiocyanate in serum (2) or can be shown to recover about 100%o of thiocyanate added to serum (3). If any thiocyanate is bound to a non-diffusible component of blood, such as protein, then the bound portion will not be free to diffuse out of the vascular compartment. Accordingly, the

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Thermodynamic Analysis for Cationic Surfactants Binding to Bovine Serum Albumin

In the present study, the binding isotherms for interaction of a homologous series of n-alkyltrimethyl ammonium bromides with bovine serum albumin (BSA) have been analyzed on basis of intrinsic thermodynamic quantities. In this regards, the intrinsic Gibbs free energy of binding, AGb(i,)„ has been estimated at various surfactant concentrations and its trend of variation for both binding sets ha...

متن کامل

Molecular dynamics simulation and docking studies on the binding properties of several anticancer drugs to human serum albumin

Disposition and transportation of anticancer drugs by human serum albumin (HSA) affects their bioavailability, distribution and elimination. In this study, the interaction of a set of anticancer drugs with HSA was investigated by molecular dynamics and molecular docking simulations. The drugs' activities were analyzed according to their docking scores, binding sites and structural descriptors. ...

متن کامل

Comparative Binding Affinities of Flavonoid Phytochemicals with Bovine Serum Albumin

Dietary flavonoids show beneficial effects in the prevention of chronic diseases. However, flavonoid bioavailability is poor, probably due to their interaction with serum albumins. In the current work, the binding interactions of eight related flavonoids, sharing a similar core structure, with bovine serum albumin (BSA) were investigated by fluorescence spectroscopy. The binding affinities of t...

متن کامل

Molecular Dynamics Simulation and Free Energy Studies on the Interaction of Salicylic Acid with Human Serum Albumin (HSA)

Human serum albumin (HSA) is the most abundant protein in the blood plasma. Molecular dynamics simulations of subdomain IIA of HSA and its complex with salicylic acid (SAL) were performed to investigate structural changes induced by the ligand binding. To estimate the binding affinity of SAL molecule to subdomains IB and IIA in HSA protein, binding free energies were calculated using the Molecu...

متن کامل

Studies of In-Vitro Amlodipine and Arsenic Displacement Interaction at Binding Sites of Bovine Serum Albumin

In this study, the binding of amlodipine (a Ca ++ channel Blocker) and arsenic (metalloid) to bovine serum albumin (BSA) was studied by equilibrium dialysis(ED) method in order to have an insight into their binding chemistry to BSA. Free amlodipine concentration was increased due to addition of arsenic which reduced the binding of the compounds to BSA. However, the free fraction was not increa...

متن کامل

Probing the Binding of Valacyclovir Hydrochloride to the Human Serum Albumin

UV-visible and Fluorescence spectroscopic methods were employed to study the interaction of human serum albumin (HSA) with Valacyclovir Hydrochloride. Additionally, molecular dynamics and molecular docking simulations were used to visualize and specify the binding site of Valacyclovir Hydrochloride. The Stern-Volmer and van't Hoff equations along with spectroscopic observations, were used to de...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:

دوره   شماره 

صفحات  -

تاریخ انتشار 2013