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

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.

Download Full-text

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

International Journal of Pharmaceutics ◽

10.1016/0378-5173(90)90212-m ◽

1990 ◽

Vol 61 (3) ◽

pp. 219-223 ◽

Cited By ~ 2

Author(s):

D JURETIC ◽

I CEPELAK ◽

V JALSENJAK ◽

T ZANICGRUBISIC ◽

K LIPOVAC ◽

...

Keyword(s):

Acetylsalicylic Acid ◽

Human Serum ◽

Serum Proteins ◽

Human Serum Proteins

Download Full-text

Determination of the Serum Unbound Fraction of Tadalafil in Children with Protein-Losing Enteropathy and Its Specific Binding to Human Serum Proteins in Vitro

Biological and Pharmaceutical Bulletin ◽

10.1248/bpb.b18-00652 ◽

2019 ◽

Vol 42 (1) ◽

pp. 110-115

Author(s):

Nanami Shigetomi ◽

Kenta Kamiya ◽

Toru Takamori ◽

Naoki Yoshimura ◽

Sayaka Ozawa ◽

...

Keyword(s):

Human Serum ◽

Serum Proteins ◽

Specific Binding ◽

Protein Losing Enteropathy ◽

Unbound Fraction ◽

Human Serum Proteins

Download Full-text

Adsorption of Human Serum Proteins on Carbonaceous Materials

Key Engineering Materials ◽

10.4028/www.scientific.net/kem.336-338.1814 ◽

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.

Download Full-text

STUDIES ON AROMATIC ESTERASE AND CHOLINESTERASE OF HUMAN SERUM

Canadian Journal of Biochemistry and Physiology ◽

10.1139/y59-151 ◽

1959 ◽

Vol 37 (1) ◽

pp. 1367-1373 ◽

Cited By ~ 6

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.

Download Full-text

Binding of toremifene to human serum proteins: Study on potential interactions between toremlfene and other highly protein-bound drugs in vitro

European Journal of Cancer ◽

10.1016/s0959-8049(97)86047-9 ◽

1997 ◽

Vol 33 ◽

pp. S251

Author(s):

S. Laakso ◽

M. Anttila

Keyword(s):

Human Serum ◽

Serum Proteins ◽

Potential Interactions ◽

Human Serum Proteins

Download Full-text

STUDIES ON AROMATIC ESTERASE AND CHOLINESTERASE OF HUMAN SERUM

Canadian Journal of Biochemistry and Physiology ◽

10.1139/o59-151 ◽

1959 ◽

Vol 37 (11) ◽

pp. 1367-1373 ◽

Cited By ~ 23

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.

Download Full-text