Differential scanning calorimetry of chromaffin granule membranes

Summary Differential scanning calorimetry thermograms of native chromaffin granule membranes exhibit several peaks in the 15–35°C region. Extraction of cholesterol increases the size of the melting peaks. Addition of Ca²⁺ ions does not seem to influence the lipid transitions.This research was supported in part by a grant from the United States-Israel Binational Science Foundation (BSF), Jerusalem, Israel. A.S. acknowledges partial support for this research from a National Science Foundation Grant PCM 04079, and from National Institutes of Health grants CA 08748 ans CA 18759.     

Differential scanning calorimetry of chromaffin granule membranes.

Differential scanning calorimetry thermograms of native chromaffin granule membranes exhibit several peaks in the 15-35 degrees C region. Extraction of cholesterol increases the size of the melting peaks. Addition of Ca2+ ions does not seem to influence the lipid transitions.     

In vitro amiodarone protein binding and its interaction with warfarin

Summary The binding of amiodarone to human plasma protein and to bovine serum, albumin was studied by three different methods, ultracentrifugation, equilibrium dialysis and fluorescence spectroscopy. The fraction of amiodarone bound to plasma protein amounted to 96.3%. The changes in the binding properties of 1-anilino-naphthalene-8-sulfonate for bovine serum albumin using warfarin and amiodarone as independent inhibitors were analyzed in terms of binding site specificity. The findings indicated that amiodarone and warfarin have two different binding sites on bovine serum albumin, so a noncompetitive inhibition mechanism was indicated. On the basis of our data we cannot exclude other mechanisms of interaction besides direct displacement of one drug by another; nevertheless, metabolite interference between amiodarone and coagulation cofactors may better explain the enhancement of warfarin's pharmacological action in association with amiodarone.This work was partially funded by the CNR (National Research Council, Rome, Italy), Program on Clinical Pharmacology and Rare Diseases. The authors would like to thanks Drs E. Marzi and E. riva for their help.     

In vitro amiodarone protein binding and its interaction with warfarin

The binding of amiodarone to human plasma protein and to bovine serum albumin was studied by three different methods, ultracentrifugation, equilibrium dialysis and fluorescence spectroscopy. The fraction of amiodarone bound to plasma protein amounted to 96.3%. The changes in the binding properties of 1-anilino-naphthalene-8-sulfonate for bovine serum albumin using warfarin and amiodarone as independent inhibitors were analyzed in terms of binding site specificity. The findings indicated that amiodarone and warfarin have two different binding sites on bovine serum albumin, so a noncompetitive inhibition mechanism was indicated. On the basis of our data we cannot exclude other mechanisms of interaction besides direct displacement of one drug by another; nevertheless, metabolite interference between amiodarone and coagulation cofactors may better explain the enhancement of warfarin's pharmacological action in association with amiodarone.     

In vitro and in vivo interaction of nuclear antibodies with corresponding antigens

Zusammenfassung Es wird mit indirekter Immunofluoreszenz gezeigt, dass Leberzellkerne mit Antikörpern bedeckt werden können, wenn sie systemischemLupus erythromatosus-Serum (SLE) für weniger als 2 sec ausgesetzt werden, und dass die Färbungsintensität vom Titer des Antikörpers abhängt.Diese Ergebnisse deuten darauf hin, dass das in SLE-Geweben durch direkte Immunofluoreszenz nachgewiesene nukleare-Globulin hauptsächlich nukleare post-Biopsiereaktionen wiederspiegelt und weniger in vivo-Reaktionen, und dass in beiden Fällen nur abgestorbene oder nicht intakte Zellen vom Antikörper durchdrungen werden.

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This investigation was supported in part by a training grant (2E-130) from the U.S. Public Health Service. Taken in part from thesis (G.W.B.) submitted to the Faculty of the Graduate School of Arts and Sciences of the University of Buffalo (N.Y., USA) in partial fulfillment of the requirements for the degree of Doctor of Philosophy (1962). Present address (G.W.B.): Department of Pathology, State University of New York at Buffalo.     

In vitro binding of citrinin to serum protein

Summary In vitro study shows that the mycotoxin citrinin binds to human serum albumin.Part of Ph. D. thesis, University of Madras, 1973.Acknowledgment is due to Dr E. R. B. Shanmugasundaram (University of Madras) and Dr J. Jayaraman (Madurai University) for kind guidance.     

In vivo and in vitro effect of sulfathiazole on serum glycoproteins

Zusammenfassung Durch Sulfathiazolzugabe in vitro oder durch Sulfathiazolbehandlung in vivo wird der Glycoproteingehalt des Albumins und der-1-Globuline reduziert.     

In vitro andin vivo activity on catalase of electrophoretically pure human serum albumin

Riassunto Albumine umane purissime dimostranoin vivo sulla catalasi epatica dei topi, una inibizione molto significativa fino alla dose di 10 mg/topo;in vitro, sulla catalasi cristallizzata, determinano un certo aumento dell'attività di difficile interpretazione.

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Acknowledgment. The present research was partially supported by a grant from Farmitalia S.p.A.     

In vitro primary immune response resulting from the interaction between bone marrow-derived and thymus cells

Riassunto Globuli rossi di pecora inducono in vitro, in colture miste di cellule spleniche di topi timectomizzati e timociti di topi normali, una risposta immune di tipo emolitico paragonabile a quella di cellule spleniche di topi normali. I dati indicano che la risposta immune delle colture miste risulta dall'interazione dell'antigene con timociti e cellule spleniche di origine midollare.

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Supported by CNEN-Euratom Association Contract. Publication No. 512 of the Euratom Biology Division.     

In vitro uncoupling of oxidative phosphorylation in normal liver mitochondria by serum of sarcoma-bearing rats

Riassunto Gli autori hanno esaminato l'influenza esercitatain vitro da parte del siero di ratti portatori di sarcoma Galliera sulla fosforilazione ossidativa in mitocondri di fegato normale. Dagli esperimenti effettuati risulta che il siero di portatore di tumore determina disaccoppiamento delle fosforilazioni dalle ossidazioni nei mitocondri di fegato normale. Gli autori, in riferimento a precedenti ricerche, discutono le probabili cause di questo fenomeno dovuto ad una sostanza o sostanze liberatesi dal tessuto neoplastico.     

Penetration and interaction with haemoglobin of Corynebacteria-like microorganisms into erythrocytes in vitro

Summary Following 24 h incubation of normal blood in the presence of the microorganism, the evolution of cell wall deficient forms within the erythrocytes and a process of oxidation of the haemoglobin may be observed.     

Penetration and interaction with haemoglobin of corynebacteria-like microorganisms into erythrocytes in vitro.

Following 24 h incubation of normal blood in the presence of the microorganism, the evolution of cell wall deficient forms within the erythrocytes and a process of oxidation of the haemoglobin may be observed.