Synthesis of cationic carbon dots and their effects on human serum proteins and in vitro blood coagulation

Luminescence ◽  
2021 ◽  
Author(s):  
Hua Qiao ◽  
Huichao Zhang ◽  
Ajab Khan ◽  
Bo Li ◽  
Lin Ge ◽  
...  
Keyword(s):  
Human Serum ◽  
Blood Coagulation ◽  
Carbon Dots ◽  
Serum Proteins ◽  
Human Serum Proteins

Reversible binding of 5- and 8-methoxypsoralen to human serum proteins (albumin) and to epidermis in vitro

1979 ◽  
Vol 101 (6) ◽  
pp. 669-677 ◽  
Author(s):  
M. ARTUC ◽  
G. STUETTGEN ◽  
W. SCHALLA ◽  
H. SCHAEFER ◽  
J. GAZITH
Keyword(s):  
Human Serum ◽  
Serum Proteins ◽  
Reversible Binding ◽  
Human Serum Proteins

A Differential Interaction of Doxorubicin and Daunorubicin with Human Serum Proteins

1981 ◽  
Vol 67 (5) ◽  
pp. 399-403 ◽  
Author(s):  
Franco Zunino ◽  
Romolo A. Gambetta ◽  
Adriano Zaccara ◽  
Roberto Carsana
Keyword(s):  
Human Serum ◽  
Reaction Mechanisms ◽  
Serum Proteins ◽  
Covalent Bond ◽  
Comparative Investigation ◽  
Experimental Conditions ◽  
Differential Interaction ◽  
Bound Drug ◽  
Human Serum Proteins

The results of a comparative investigation on the interaction of doxorubicin (adriamycin) and daunorubicin with serum proteins are reported. Whereas a strong interaction occurs in vitro between doxorubicin and human serum proteins, no appreciable binding to proteins could be detected for daunorubicin under similar experimental conditions. Since the protein-bound drug is only partially dissociated by physical procedures including gel-electrophoresis, column-chromatography and solvent extraction, the formation of a covalent bond is suggested. The doxorubicin binding to serum proteins is apparently nonselective for a class of proteins; it is strongly reduced in acid conditions and slightly dependent on the ionic strenght. Two tentative reaction mechanisms have been considered.

Effect of microencapsulated acetylsalicylic acid on glycosylation of human serum proteins in vitro

1990 ◽  
Vol 61 (3) ◽  
pp. 219-223 ◽  
Author(s):  
D JURETIC ◽  
I CEPELAK ◽  
V JALSENJAK ◽  
T ZANICGRUBISIC ◽  
K LIPOVAC ◽  
...  
Keyword(s):  
Acetylsalicylic Acid ◽  
Human Serum ◽  
Serum Proteins ◽  
Human Serum Proteins

Adsorption of Human Serum Proteins on Carbonaceous Materials

2007 ◽  
Vol 336-338 ◽  
pp. 1814-1817
Author(s):  
B.G. Li ◽  
Yun Qing Kang ◽  
Guang Fu Yin ◽  
Chang Qiong Zheng
Keyword(s):  
Human Serum ◽  
Competitive Adsorption ◽  
Serum Proteins ◽  
Blood Compatibility ◽  
Carbon Film ◽  
Adsorption Ability ◽  
Rational Explanation ◽  
Labeling Method ◽  
Human Serum Proteins

In this paper, the adsorption of human serum albumin (HSA), human serum fibrinogen (HFG) and human serum immune globulin (IG) on surfaces of diamond like carbon film (DLC), diamond film (DF) and graphite has been studied. The adsorption isotherms of single component protein solution and the competitive adsorption of binary system have been investigated by radioisotope 125 I labeling method. Results showed that (1) the adsorptive amounts of HSA on DLC is more than that of HFG, but the adsorptive amounts of HFG on DF and graphite are apparently more than those HSA; (2) the relative competitive adsorption ability of three proteins on DF and graphite surfaces is HFG > IG > HSA, but that on DLC is HFG ≈ HAS > IG, comparison with HSA, there is no apparent competitive adsorption superiority on DLC for HFG. These results indicated that there is no apparent distinction for the adsorption of three human serum proteins on DLC, but the adsorption of HFG on DF and graphite takes precedence in varying degrees. It probably makes rational explanation for the result of blood-compatibility tests in vitro that DLC is good, but DF and graphite are worse.

STUDIES ON AROMATIC ESTERASE AND CHOLINESTERASE OF HUMAN SERUM

1959 ◽  
Vol 37 (1) ◽  
pp. 1367-1373 ◽  
Author(s):  
A. Marton ◽  
W. Kalow
Keyword(s):  
Human Serum ◽  
Esterase Activity ◽  
Staining Method ◽  
Serum Proteins ◽  
Close Relation ◽  
Strong Inhibition ◽  
Ultraviolet Spectrophotometry ◽  
Normal Controls ◽  
Human Serum Proteins

Human serum proteins were separated by electrophoresis on filter paper. Cholinesterase could not be readily eluted from the paper but was demonstrated to be between α2- and β-globulins by a staining method. Aromatic esterase migrated in close relation to albumin and could be eluted by M/15 phosphate buffer of pH 7.4. The esterase activity was demonstrated in the eluates by ultraviolet spectrophotometry, using phenylacetate as a substrate. Versene caused a strong inhibition of aromatic esterase activity in vitro. The activity could be restored by different cations of which Ca++, Cu++, and Mn++were most potent. In 74 persons who were considered as normal controls in regard to the esterases, there was no correlation between cholinesterase and aromatic esterase activity. However, in 25 individuals suffering from cancer and/or liver dysfunction, a significant correlation between the two enzyme activities appeared.

STUDIES ON AROMATIC ESTERASE AND CHOLINESTERASE OF HUMAN SERUM

1959 ◽  
Vol 37 (11) ◽  
pp. 1367-1373 ◽  
Author(s):  
A. Marton ◽  
W. Kalow
Keyword(s):  
Human Serum ◽  
Esterase Activity ◽  
Staining Method ◽  
Serum Proteins ◽  
Close Relation ◽  
Strong Inhibition ◽  
Ultraviolet Spectrophotometry ◽  
Normal Controls ◽  
Human Serum Proteins

Human serum proteins were separated by electrophoresis on filter paper. Cholinesterase could not be readily eluted from the paper but was demonstrated to be between α2- and β-globulins by a staining method. Aromatic esterase migrated in close relation to albumin and could be eluted by M/15 phosphate buffer of pH 7.4. The esterase activity was demonstrated in the eluates by ultraviolet spectrophotometry, using phenylacetate as a substrate. Versene caused a strong inhibition of aromatic esterase activity in vitro. The activity could be restored by different cations of which Ca++, Cu++, and Mn++were most potent. In 74 persons who were considered as normal controls in regard to the esterases, there was no correlation between cholinesterase and aromatic esterase activity. However, in 25 individuals suffering from cancer and/or liver dysfunction, a significant correlation between the two enzyme activities appeared.

scholarly journals Binding of Human Serum Proteins to Titanium Dioxide Particles In Vitro

2011 ◽  
Vol 53 (2) ◽  
pp. 75-83 ◽  
Author(s):  
Mazen S.K. Zaqout ◽  
Tomoyuki Sumizawa ◽  
Hideki Igisu ◽  
Toshiaki Higashi ◽  
Toshihiko Myojo
Keyword(s):  
Titanium Dioxide ◽  
Human Serum ◽  
Serum Proteins ◽  
Human Serum Proteins
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