Binding of indole-acetic acid to cytosol proteins of embryonic chicken liver

3H-Indole acetic acid bound to cytosol proteins of embryonic chicken liver in vitro to an average capacity of at least 20 pmoles/mg binding protein. The auxin-binding protein complexes could be resolved into 4 major zones by anion exchange chromatography; they sedimented at 3-7 S in sucrose density gradients, and were also heterogenous in agarose gel electrophoresis.     

Effect of acute administration of triiodothyronine in chicken. Liver glycogen depletion and amino acid incorporation to proteins

Summary Single injections of thyroid hormone (T₃) produce liver glycogen depletion in chickens. This effect cannot be suppressed by protein synthesis inhibitors and is previous to the hormone-induced increase in protein synthesis.     

Binding of D-alpha-tocopherol to rat liver nuclear components.

When D-alpha-tocopherol is administered i.v. to vitamin E deficient rats, significant amounts of this vitamin are bound to a nucleoprotein complex in hepatic nuclei, and this complex can be solubilized by high concentrations of sodium chloride (0.6 M). The bound vitamin in this complex, extractable by ethanol, was found to be identical with authentic alpha-tocopherol by thin layer chromatography.     

Binding of centchroman--a nonsteroidal antifertility agent to human plasma proteins

Centchroman, a non-steroidal antifertility agent showed a low affinity (Kd = 13.19 X 10(-6) M) and nonsaturable binding to human plasma. Centchroman did not compete either with sex hormone binding globulin or corticosteroid binding globulin. Polyacrylamide gel electrophoresis and temperature dependent binding characteristics revealed that the protein responsible for centchroman binding to human plasma resembles albumin.     

sRNA methylase activity of embryonic liver

Résumé Utilisant SAM-¹⁴CH₃ il a été démontré que le foie foetal a plus d'activité de sRNA methylase que le foie adulte.

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This investigation was supported in part by an allocation from a Public Health Service General Research Support Grant No. SO 1 FR-05545-03, and an American Cancer Society Grant No. IN 19F to The Jackson Laboratory, Bar Harbor, Maine, and by Public Health Service Research Grants No. HD-01496 from the National Institute of Child Health and Human Development and No. FR-00251 from the Division of Research Facilities and Resources.     

Binding property of rat andLimulus C-reactive proteins (CRP) to mercury

Summary The C-reactive proteins (CRP) from both rat andLimulus were found to bind mercury (Hg) in both in vivo and in vitro conditions. CRP has high-affinity binding sites for Hg as evidenced by the loss of free sulfhydryl groups, arrested mobility in polyacrylamide gel electrophoresis, and the consumption of CRP in the serum after Hg administration. The binding was tight as it could not be inhibited either by the addition of cysteine or EDTA. By using a direct titration method it was shown that binding of Hg to CRP was saturable at a molar ratio of Hg/CRP=13.11. The possibility that CRP may act as a scavenger for Hg is discussed.     

Binding of aflatoxins B1 and G1 to human serum proteins

Zusammenfassung In vitro Experimente mit¹⁴C-markiertem, gereinigtem Aflatoxin zur Untersuchung der Bindung von Aflatoxin B₁ und G₁ an verschiedene Serumproteine ergaben, dass Aflatoxin B₁ hauptsächlich mit-Globulin, G₁ dagegen vorwiegend mit Albumin bindet.

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This work was supported by part by a grant from the China Medical Board of New York, Inc., and was performed during one of us (S.S.L.) received a class C. research award from the National Science Council, Republic of China.     

Binding of centchroman—a nonsteroidal antifertility agent to human plasma proteins

Summary Centchroman, a non-steroidal antifertility agent showed a low affinity (K_d=13.19×10^–6 M) and nonsaturable binding to human plasma. Centchroman did not complete either with sex hormone binding globulin or corticosteroid binding globulin. Polyacrylamide gel electrophoresis and temperature dependent binding characteristics revealed that the protein responsible for centchroman binding to human plasma resembles albumin.Acknowledgment. The authors are grateful to Dr. Nitya Nand for his interest in this investigation. CDRI Communication No. 3333.     

Binding of tryptophan to different serum proteins in humans and in rats

Riassunto Sieri di uomo e di ratto sono stati incubati con C¹⁴-l-triptofano e sottoposti a elettroforesi su gel di poliacrilamide. Nel siero umano la radioattività si è localizzata nelle frazioni albuminica, prealbuminica e macroglobulinica. Nel siero di ratto il C¹⁴-l-triptofano si è localizzato nella zona delle albumine, -globuline e macroglobuline.