Kinetic and thermodynamic analysis of 9-nitrocamptothecin hydrolysis at physiological pH in the presence and absence of human serum albumin

2010 ◽  
Vol 42 (12) ◽  
pp. 693-703 ◽  
Author(s):  
Sohodeb C. Saha ◽  
Sasank Kunadharaju ◽  
Balasubramanian Sivakumar ◽  
Michalakis Savva
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Thermodynamic Analysis ◽  
Presence And Absence ◽  
Kinetic And Thermodynamic Analysis

Potassium sorbate as an AGE activator for human serum albumin in the presence and absence of glucose

2013 ◽  
Vol 62 ◽  
pp. 146-154 ◽  
Author(s):  
F.Taghavi ◽  
A.A. Moosavi-Movahedi ◽  
M. Bohlooli ◽  
H. Hadi Alijanvand ◽  
M. Salami ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Potassium Sorbate ◽  
Presence And Absence

scholarly journals Pb2+, Cu2+, Zn2+, Mg2+ and Mn2+ reduce the affinities of flavone, genistein and kaempferol for human serum albumin in vitro

2011 ◽  
Vol 63 (3) ◽  
pp. 623-634 ◽  
Author(s):  
Fan Yang ◽  
Jie Wang ◽  
Chunxi Liu ◽  
Xu Xiaochen ◽  
Li Wenjun ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Metal Ions ◽  
Human Serum ◽  
Blue Shift ◽  
Red Shift ◽  
Presence And Absence

Flavone (Fl), genistein (Gen) and kaempferol (Kol) were studied for their affinities towards human serum albumin (HSA) in the presence and absence of Pb2+,Cu2+,Zn2+,Mg2+ and Mn2+. The fluorescence intensities of HSA decreased with increasing concentration of the three flavonoids. Kaempferol resulted in a blue-shift of the ?em of HSA from 336 to 330 nm; flavone showed an obvious red-shift of the ?em of HSA from 336 to 342 nm; genistein did not cause an obvious blue-shift or red-shift of the ?em of HSA. However, the extents of ?em-shifts induced by the flavonoids in the presence of metal ions were much bigger than that in the absence of mental ions. Pb2+,Cu2+,Zn2+,Mg2+ and Mn2+ reduced the quenching constants of the flavonoids for HSA by 14.6% to 60.7% , 28% to 67.9%,3.5% to 59.4%, 23.2% to 63.7% and 14% to 65%, respectively. The affinities of flavone, genistein and kaempferol for HSA decreased about 10.84%, 10.05%and 3.56% in the presence of Pb2+, respectively. Cu2+ decreased the affinities of flavone, genistein and kaempferol for HSA about 14.04%, 5.14%and 8.89%, respectively. Zn2+ decreased the affinities of flavone, genistein and kaempferol for HSA about 3.79%, 0.55% and 3.58%, respectively. Mg2+ decreased the affinities of flavone, genistein and kaempferol for HSA about 16.94%, 2.94%and 7.04%, respectively. Mn2+ decreased the affinities of flavone, genistein and kaempferol for HSA about 14.24%, 3.66% and 4.78%, respectively.

Biochemical, biophysical, and thermodynamic analysis of in vitro glycated human serum albumin

2007 ◽  
Vol 72 (2) ◽  
pp. 146-152 ◽  
Author(s):  
Mohd. Wajid Ali Khan ◽  
Zafar Rasheed ◽  
Wahid Ali Khan ◽  
Rashid Ali
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Thermodynamic Analysis

scholarly journals Reaction of the Anticancer Organometallic Ruthenium Compound, [(η6-p-Cymene)Ru(ATSC)Cl]PF6 with Human Serum Albumin

2010 ◽  
Vol 2010 ◽  
pp. 1-7 ◽  
Author(s):  
Floyd A. Beckford
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Thermodynamic Analysis ◽  
Binding Constant ◽  
Enthalpy Of Reaction ◽  
Infrared Spectrophotometry ◽  
Ruthenium Compound ◽  
Different Temperatures ◽  
Entropy Of Reaction

The reaction of [(η6-p-cymene)Ru(ATSC)Cl]PF6 (ATSC =9-anthraldehyde thiosemicarbazone) with human serum albumin was investigated at different temperatures using fluorescence and infrared spectrophotometry. The binding constant, K, for the reaction was determined using a number of different methods. Using a modified Stern-Volmer equation, K was determined to be 9.09×104,12.1×104, and 13.1×104 M−1 at 293 K, 298 K, and 308 K, respectively. A thermodynamic analysis showed that the reaction is spontaneous with ΔG being negative. The enthalpy of reaction ΔH=16.5 kJ mol−1 and the entropy of reaction ΔS=152 Jmol−1K−1. The values of ΔH and ΔS suggest that hydrophobic forces are dominant in the mode of interaction and that the process is mostly entropy driven.

Natural peptide anti-glycation effect in the presence of Aloe vera phenolic components on human serum albumin

RSC Advances ◽  
2015 ◽  
Vol 5 (1) ◽  
pp. 248-254 ◽  
Author(s):  
Ali Akbar Moosavi-Movahedi ◽  
Fatemeh Ghamari ◽  
Seyed Mahmoud Ghaffari ◽  
Maryam Salami ◽  
Farzaneh Farivar ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Aloe Vera ◽  
Phenolic Components ◽  
Natural Peptide ◽  
Presence And Absence

This study explores the anti-glycation effect of aloin, in the presence and absence of casein-derived peptides, on human serum albumin HSA.

Thermodynamic Analysis of the Interaction between Cationic Porphyrins and Human Serum Albumin by an Optical Biosensor

2005 ◽  
Vol 23 (8) ◽  
pp. 1095-1099 ◽  
Author(s):  
Qin Yi-Min ◽  
Pan Ni-Na ◽  
Jian Yong-Xing ◽  
Li Zao-Ying ◽  
Zou Guo-Lin
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Thermodynamic Analysis ◽  
Optical Biosensor ◽  
Cationic Porphyrins
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