Binding of Oxovanadium(IV) Complexes to Blood Serum Albumins
نویسندگان
چکیده
منابع مشابه
Binding of bromosulphthalein to serum albumins.
The binding of bromosulphthalein to human and bovine Serum albumin was studied by infrared spectroscopy, laser-Raman spectroscopy, visible spectroscopy and pH measurements in order to obtain information on the binding forces involved. No conformational change of the proteins was observed during the tight binding of the first three bromosulphthalein molecules as indicated by the kinetics of the ...
متن کاملAldolase activity of serum albumins.
Bovine and human serum albumins catalyze the aldol reaction of aromatic aldehyedes and acetone, with saturation kinetics and moderate and opposite enantioselectivity. The reaction occurs at the binding site in domain IIa, and is inhibited by warfarin. Kinetic data are consistent with an enamine mechanism. The activity is conserved in a 103 aminoacid peptide derived from the albumin sequence.
متن کاملBinding of Sulpiride to Seric Albumins
The aim of this work was to study the interaction of sulpiride with human serum albumin (HSA) and bovine serum albumin (BSA) through the fluorescence quenching technique. As sulpiride molecules emit fluorescence, we have developed a simple mathematical model to discriminate the quencher fluorescence from the albumin fluorescence in the solution where they interact. Sulpiride is an antipsychotic...
متن کاملBINDING OF THE ANTITUMOR DRUG ADRIAMYCIN TO DNA-HISTONE COMPLEXES
Isotherms of the binding of the anthracycIine antibiotic, adriamycin (adriblastin), to DNA histone complexes was studied by means of spectroscopic analysis. The results indicated that: (a) binding of adriamycin to histones reduced the interaction of histones with DNA, (b) binding of the drug to DNA did not change the binding affinity of histone to DNA and, (c) in the explored binding range...
متن کاملThe binding of L-tryptophan to serum albumins in the presence of non-esterified fatty acids.
Bovine, human and rat serum albumins were defatted and palmitic acid, oleic acid and lauric acid added in various molar ratios. The binding of L-tryptophan to these albumins was measured at 20 degrees C in a 0.138 M salt solution at pH 7.4, by using an ultrafiltration technique, and analysed in terms of n, the number of available tryptophan-binding sites per albumin molecule, with apparent asso...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Journal of the Mexican Chemical Society
سال: 2017
ISSN: 2594-0317,1870-249X
DOI: 10.29356/jmcs.v57i3.205