Abstract
In man, sul f aphenazole has a lower affinity for the albumin o f the fetus and neonate than for that of the adult. Removal of bound endogenous anions from neonatal albumin by treatment with charcoal at pH 3.0 restored the affinity of the protein for sulfaphenazole to the adult level. Prior treatment of adult albumin with bilirubin reduced the affinity of the protein for sulfaphenazole to that observed in fetal and neonatal albumins. Thus the reduced affinity of sulfaphenazole for fetal and neonatal albumin compared to that for adult albumin probably is the result o f the presence o f a tightly bound endogenous ligand, such as bilirubin, on fetal and neonatal albumin.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 897-901 |
| Number of pages | 5 |
| Journal | Clinical pharmacology and therapeutics |
| Volume | 12 |
| Issue number | 6 |
| DOIs | |
| State | Published - Jan 1 1971 |
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All Science Journal Classification (ASJC) codes
- Pharmacology
- Pharmacology (medical)
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The binding of sulfaphenazole to fetal, neonatal, and adult human plasma albumin. / Chignell, Colin F.; Vesell, Elliot S.; Starkweather, Donnas K.; Berlin, Cheston M.
In: Clinical pharmacology and therapeutics, Vol. 12, No. 6, 01.01.1971, p. 897-901.Research output: Contribution to journal › Article
TY - JOUR
T1 - The binding of sulfaphenazole to fetal, neonatal, and adult human plasma albumin
AU - Chignell, Colin F.
AU - Vesell, Elliot S.
AU - Starkweather, Donnas K.
AU - Berlin, Cheston M.
PY - 1971/1/1
Y1 - 1971/1/1
N2 - In man, sul f aphenazole has a lower affinity for the albumin o f the fetus and neonate than for that of the adult. Removal of bound endogenous anions from neonatal albumin by treatment with charcoal at pH 3.0 restored the affinity of the protein for sulfaphenazole to the adult level. Prior treatment of adult albumin with bilirubin reduced the affinity of the protein for sulfaphenazole to that observed in fetal and neonatal albumins. Thus the reduced affinity of sulfaphenazole for fetal and neonatal albumin compared to that for adult albumin probably is the result o f the presence o f a tightly bound endogenous ligand, such as bilirubin, on fetal and neonatal albumin.
AB - In man, sul f aphenazole has a lower affinity for the albumin o f the fetus and neonate than for that of the adult. Removal of bound endogenous anions from neonatal albumin by treatment with charcoal at pH 3.0 restored the affinity of the protein for sulfaphenazole to the adult level. Prior treatment of adult albumin with bilirubin reduced the affinity of the protein for sulfaphenazole to that observed in fetal and neonatal albumins. Thus the reduced affinity of sulfaphenazole for fetal and neonatal albumin compared to that for adult albumin probably is the result o f the presence o f a tightly bound endogenous ligand, such as bilirubin, on fetal and neonatal albumin.
UR - http://www.scopus.com/inward/record.url?scp=0015156051&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0015156051&partnerID=8YFLogxK
U2 - 10.1002/cpt1971126897
DO - 10.1002/cpt1971126897
M3 - Article
C2 - 5134994
AN - SCOPUS:0015156051
VL - 12
SP - 897
EP - 901
JO - Clinical Pharmacology and Therapeutics
JF - Clinical Pharmacology and Therapeutics
SN - 0009-9236
IS - 6
ER -