scholarly journals (E)-2-Benzylidenecycloalkanones XII.* Kinetic Measurement of Bovine and Human Serum Albumine Interaction with Selected Chalcones and Their Cyclic Chalcone Analogues by UV Spectrophotometry

2015 ◽  
Vol 03 (01) ◽  
pp. 1-8 ◽  
Author(s):  
Beáta Veliká ◽  
Vladimíra Tomečková ◽  
Krisztina Fodor ◽  
Ivan Kron ◽  
Pál Perjési
Keyword(s):  
Human Serum ◽  
Uv Spectrophotometry ◽  
Kinetic Measurement ◽  
Cyclic Chalcone Analogues

Determination of fleroxacin in human serum and in dosage forms by derivative UV spectrophotometry

1998 ◽  
Vol 18 (1-2) ◽  
pp. 145-150 ◽  
Author(s):  
Milena Jelikic-Stankov ◽  
Jadranka Odovic ◽  
Dejan Stankov ◽  
Predrag Djurdjevic
Keyword(s):  
Human Serum ◽  
Dosage Forms ◽  
Uv Spectrophotometry ◽  
Derivative Uv Spectrophotometry

The Effects of 1-Propanol on Behaviour of Human Serum Albumin in Alkaline Solution

1993 ◽  
Vol 58 (2) ◽  
pp. 267-280
Author(s):  
Vladimír Karpenko ◽  
Rostislav Škrabana
Keyword(s):  
Fatty Acids ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Conformational Transition ◽  
Point Of View ◽  
Uv Spectrophotometry ◽  
Fourth Derivative ◽  
Ph Range ◽  
Albumin Molecule

The effects of 1-propanol ant to a certain extent of ethanol on human serum albumin were studied over the pH range 7 - 13.3 and alcohol concentrations up to 20 vol.%. In some case behaviour of the native preparation was compared with albumin cleared of weaker bound fatty acids. The data obtained by UV-spectrophotometry were discussed from the point of view of individual types of chromophores as well as in a broader context of the secondary structure. The results can be summarized as follows: (a) Partial removal of bound fatty acids has an influence on the dissociation of tyrosines. (b) The effect of alcohols on this dissociation is rather complex, the permitivity of the solvent being only a part of it. (c) At high alkaline pH a series of peaks in the fourth-derivative absorption spectra appear in the region 305 - 320 nm. These peaks were shown to correspond to buried dissociated tyrosines. (d) In the presence of 1-propanol a small conformational transition of albumin molecule is observed at pH below 9.

Mechanism of denaturation of human serum albumin by urea

1988 ◽  
Vol 53 (2) ◽  
pp. 411-422 ◽  
Author(s):  
Josef Chmelík ◽  
Pavel Anzenbacher ◽  
Jitka Chmelíková ◽  
Milada Matějčková ◽  
Vítěz Kalous
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Disulfide Bonds ◽  
Polyacrylamide Gel Electrophoresis ◽  
Helical Structure ◽  
Random Coil ◽  
Gel Chromatography ◽  
Uv Spectrophotometry ◽  
Comparison Of The Results

The mechanism of denaturation of human serum albumin by urea was examined by polarography, polarimetry, circular dichroism, UV-spectrophotometry, gel chromatography, and polyacrylamide gel electrophoresis. Comparison of the results obtained by these methods shows that this reaction is a complex process which cannot be described by a two-state denaturation model. It has been demonstrated that the different states which denaturation produces arise under different denaturation conditions. The different behavior of various species of human serum albumin (monomer, mercaptalbumin and nonmercaptalbumin) during denaturation by urea was examined. As a result the following probable denaturation scheme was proposed: The denaturation of human serum albumin by urea is regarded as a stepwise process involving one stable intermediary product at least ( demonstrated electrophoretically). After the rapid initial change of the ordered helical structure extensive hydrophobic domains of the molecule remain folded. Cystine residues are gradually liberated from these domains. Denaturated mercaptalbumin has the conformation of a random coil in which the pairing of native disulfide bonds has been altered because of SH-S-S interchange reactions; in contrast native disulfide bonds are retained in nonmercaptalbumin.

Development of a method to determine caffeine in human serum by HPLC

2015 ◽  
Vol 48 (06) ◽  
Author(s):  
C Rothammer ◽  
E Haen
Keyword(s):  
Human Serum
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