Degradation of Melphalan in Aqueous Solutions—Influence of Human Albumin Binding

Cloxacillin is usually given to newborn infants with sepsis in particular for penicillinase-producing staphylococcus aureus. The effect of cloxacillin on bilirubin-albumin binding was investigated in vitro using the peroxidase oxidation method with human albumin (bilirubin 0.255 mM, albumin 0.45 mM, billalb 0.56, pH 7.4, temperature 3 0°C). Sulfisoxazole, a drug which is capable of displacing bilirubin from albumin was used as control. The displacement constant of cloxacillin was 4.86 x 1o5 Nr1, stronger than that of sulfisoxazole (1. 72 x 104 M-1). Both drugs were capable of displacing bilirubin as determined by their maximal displacement factors of 2.21 and 2.29, respectively. Since cloxacillin apparently increases the risk of bilirubin encephalopathy the use of this drug in jaundiced newborns with sepsis, especially in the premature infants, should be reconsidered.

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Transport of Cortisol-4-C14 and Progesterone-4-C14 by Serum Proteins as Demonstrated by Paper Electrophoresis and Paper Chromatography

American Journal of Physiology-Legacy Content ◽

10.1152/ajplegacy.1956.185.1.54 ◽

1956 ◽

Vol 185 (1) ◽

pp. 54-60 ◽

Cited By ~ 11

Author(s):

Ulrich Westphal ◽

Hilliard E. Firschein ◽

Eli M. Pearce

Keyword(s):

Serum Proteins ◽

Critical Evaluation ◽

Paper Electrophoresis ◽

Human Albumin ◽

Albumin Binding ◽

Albumin Solution ◽

Binding Studies ◽

Rat Serum ◽

Low Concentrations ◽

Human Serum Albumin Solution

Interaction between low concentrations of cortisol-4-C14 or progesterone-4-C14 and serum proteins was investigated by paper-electrophoretic methods in human serum albumin solution as well as in human and rat serum. Between 2 and 10% of cortisol and between 70 and 90% of progesterone were found to be bound and thus transported by human albumin. Similar transport values were observed in paper-chromatographic studies in which the steroids migrated in aqueous solution, in the presence and absence of serum proteins. A critical evaluation was made on the use of paper-electrophoretic procedures in protein-binding studies. The demonstration of a firm albumin binding of progesterone, and a comparatively loose attachment of cortisol, is in general agreement with results obtained by ultracentrifugation and ‘free’ electrophoresis. Some physiological implications are mentioned.

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Albumin binding capacity is impaired in decompensated liver cirrhosis and dysfunction is reversed by targeted in vivo 20% human albumin solution infusions

Journal of Hepatology ◽

10.1016/s0168-8278(17)31132-7 ◽

2017 ◽

Vol 66 (1) ◽

pp. S390

Author(s):

L. China ◽

A. Maini ◽

D. Gilroy ◽

A. O’Brien

Keyword(s):

Liver Cirrhosis ◽

Binding Capacity ◽

Human Albumin ◽

Albumin Binding ◽

Albumin Solution ◽

Decompensated Liver Cirrhosis ◽

Human Albumin Solution

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Degradation of chlorambucil in aqueous solution-influence of human albumin binding

Journal of Pharmacy and Pharmacology ◽

10.1111/j.2042-7158.1981.tb13787.x ◽

1981 ◽

Vol 33 (1) ◽

pp. 313-315 ◽

Cited By ~ 20

Author(s):

H. Ehrsson ◽

U. Lönroth ◽

I. Wallin ◽

M. Ehrnebo ◽

S. O. Nilsson

Keyword(s):

Aqueous Solution ◽

Human Albumin ◽

Albumin Binding

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Demonstration of a firm association between hepatitis B surface antigen proteins bearing polymerized human albumin binding sites and core-specific determinants in serum hepatitis B viral particles

Molecular Immunology ◽

10.1016/0161-5890(85)90047-1 ◽

1985 ◽

Vol 22 (11) ◽

pp. 1279-1287 ◽

Cited By ~ 13

Author(s):

Marie-Anne Petit ◽

Francis Capel ◽

Jacques Pillot

Keyword(s):

Hepatitis B ◽

Surface Antigen ◽

Binding Sites ◽

Hepatitis B Surface Antigen ◽

Human Albumin ◽

Albumin Binding ◽

Serum Hepatitis ◽

Viral Particles

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"Unbound analog" radioimmunoassays for free thyroxin measure the albumin-bound hormone fraction.

Clinical Chemistry ◽

10.1093/clinchem/29.7.1408 ◽

1983 ◽

Vol 29 (7) ◽

pp. 1408-1410 ◽

Cited By ~ 53

Author(s):

J R Stockigt ◽

V Stevens ◽

E L White ◽

J W Barlow

Keyword(s):

Human Serum Albumin ◽

Serum Albumin ◽

Human Serum ◽

Equilibrium Dialysis ◽

Human Albumin ◽

Albumin Binding ◽

Free T4 ◽

One Step

Abstract We have assessed the influence of albumin-bound thyroxin (T4) on apparent free T4 values obtained by two "unbound analog" free T4 methods (AmerlexR Free T4 and Clinical Assays one-step Free T4). We evaluated sera showing three different albumin anomalies: total hereditary analbuminemia, partially corrected analbuminemia, and familial dysalbuminemic hyperthyroxinemia, where abnormal albumin-binding of analog tracer is associated with high apparent free T4 values by these methods. In hereditary analbuminemia, free T4 was almost undetectable by both assays; in contrast, free T4 by equilibrium dialysis was normal. After addition of T4-free human serum albumin, the apparent free T4 concentration in total hereditary analbuminemia became normal by the analog methods. Immunoprecipitation of [125I]T4 and the unidentified labeled kit analogs by antiserum to human albumin was negligible in untreated total hereditary analbuminemia and approximately twice normal in familial dysalbuminemic hyperthyroxinemia. Therefore, alterations in tracer binding to albumin correlate with the apparent free T4 concentrations obtained by the analog methods. The interactions of the unidentified analog tracers and T4 with albumin are such that these techniques principally reflect the albumin-bound T4 moiety.

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