Improved separation at low temperature of glycoproteins by Con A-Sepharose affinity chromatography in the presence of sodium dodecyl sulfate (SDS)

Summary The Con A-Sepharose affinity chromatography of glycoproteins was even more effective at 4°C than that at room temperature (26–28°C) in the presence of sodium dodecyl sulfate (SDS). Application of this methodology to the seperation of several glycoproteins from SDS-solubilized membrane proteins in rat cerebellum, including a glycoprotein characteristics of the Purkinje cells, was sucessful.Acknowledgments. A part of this research was supported by a Grantin-Aid for Scientific Research from the Ministry of Education, Science and Culture (No. 58480150), and also by a grant from National Center of Nervous, Mental and Muscular Disorders (NCNMMD) of the Ministry of Health and Welfare (No.83-11) in Japan.     

Improved separation at low temperature of glycoproteins by Con A-Sepharose affinity chromatography in the presence of sodium dodecyl sulfate (SDS)

The Con A-Sepharose affinity chromatography of glycoproteins was even more effective at 4 degrees C than that at room temperature (26-28 degrees C) in the presence of sodium dodecyl sulfate (SDS). Application of this methodology to the separation of several glycoproteins from SDS-solubilized membrane proteins in rat cerebellum, including a glycoprotein characteristic of the Purkinje cells, was successful.     

Effect of low density lipoprotein and high density lipoprotein on sodium dodecyl sulphate precipitation of very low density lipoprotein from human serum

Summary In the presence of low density lipoprotein, the sodium sodecyl sulphate(SDS)-very low density lipoprotein(VLDL) complex sedimented, while in the presence of high density lipoprotein the complex floated. This SDS-VLDL aggregate floats at serum triglyceride to cholesterol ratio of 0.7–0.9 and sediments at a ratio of 0.2–0.5.     

Effect of low density lipoprotein and high density lipoprotein on sodium dodecyl sulphate precipitation of very low density lipoprotein from human serum.

In the presence of low density lipoprotein, the sodium sodecyl sulphate(SDS)-very low density lipoprotein(VLDL) complex sedimented, while in the presence of high density lipoprotein the complex floated. This SDS-VLDL aggregate floats at serum triglyceride to cholesterol ratio of 0.7-0.9 and sediments at a ratio of 0.2-0.5.     

A negative cooperative binding process between chloramphenicol and sodium dodecyl sulphate to bovine serum albumin: A possible effect on drug absorption

Résumé L'étude de l'influence de concentrations prémicellaires des tensioactifs sur l'interaction BSA-CAF permet de conclure qu'il s'agit d'un mécanisme cooperatif suivant le modèle allosterique proposé parMonod, Wyman etChangeux. Ce mécanisme représente une possible explication de l'influence des tensioactifs sur l'absorption des médicaments.

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This work was supported by a C.N.R. Research Grant.     

Disc electrophoresis of fractions of bovine central nervous system myelin

Zusammenfassung Fraktionen der weissen Hirnsubstanz, die offenbar zu den hauptsächlichsten Dichtelinien des Myelins respektive zur interperiodischen Linie gehören, wurden elektrophoretisch untersucht. Die Na-Fraktionen (interperiodische Linie; Membranseite zum extrazellulären Raum) enthalten meistens saure Proteine, während die CNS- und R-Fraktionen (Hauptlinie; Membranseite zum Zellinnern) zur Hauptsache alkalische Komponenten aufweisen.     

Action of sodium dodecyl sulfate on electron transport enzymes ofRhodospirillum rubrum

Zusammenfassung SDS hat die gleiche solubilisierende Wirkung auf das Membransystem vonRhodospirillum rubrum wie DOC und Triton X-100. NADH- und Succinat-Cytochrom-c-Reduktase des partikulären Elektronentransportsystems zeigen in Gegenwart von SDS jedoch ein sowohl von DOC als auch von Triton X-100 verschiedenes Aktivierungs-Inaktivierungsverhalten. Eine direkte Wirkung von SDS auf die beiden Flavoproteine NADH-. und Succinat-Dehydrogenase im getrennten Anfangsbereich der Elektronentransportkette ist unwahrscheinlich.

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Supported by hte Deutsche Forschungsgemeinschaft and by hte stifftung Volkswagenwek. The author wishes to thank Prof. Dr. G. Drews for his interest in the work     

Paper electrophoresis of the soluble proteins of the central nervous tissue

Riassunto Le proteine idrosolubili estratte dal sistema nervoso di ratti sono state separate mediante elettroforesi su carta.Il quadro elettroforetico appare costantemente riproducibile nelle condizioni sperimentali impiegate.     

Paper electrophoresis separation of the soluble proteins of rat muscle sarcosomes

Riassunto Viene descritta la presenza, nel succo dei sarcosomi del muscolo di ratto, di 4 componenti proteici separabili mediante elettroforesi su carta. I 4 componenti sono rappresentati nella misura di rispettivamente 26.1, 18.4, 33.2 e 22.3 per 100 delle proteine totali.     

Paper electrophoresis of soluble proteins from regenerating rat liver

Riassunto Gli autori hanno studiato il comportamento delle proteine e delle glicoproteine solubili del fegato rigenerante di ratto mediante l'elettroforesi su carta. La colorazione con Amidoschwarz mostra che il comportamento elettroforetico delle proteine di fegato rigenerante è praticamente sovrapponibile a quello del fegato normale. La colorazione secondoKöiw eGrönwall dimostra che le glicoproteine diminuiscono nei primi giorni dopo l'atto operatorio, tornando però alla normalità circa 30 giorni dopo l'epatectomia.

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This investigation was aided by a grant from C.N.R., Rome, and was done during the tenure by one of us (G. G.) of a Scholarship from C.N.R., Rome.     

Paper electrophoresis of soluble proteins of rat liver mitochondria

Riassunto Mediante elettroforesi su carta si dimostra la presenza nei lisati di mitocondri di fegato di ratto di almeno 5 componenti proteici. Le colorazioni specifiche dimostrano la presenza di 3 frazioni lipoproteiche e di altrettante glicoproteiche. I lisati dei mitocondri vennero ottenuti qer trattamento delle particelle con Triton X-100.     

Interference of sodium ethylenediaminetetraacetate in the determination of proteins and its elimination

Zusammenfassung Es wird die Interferenz von Natrium Ethylendiaminotetraacetat bei der Eiweissbestimmung nach der Methode vonLowry et al. und deren Verhinderung gezeigt. Die Anwesenheit von Natrium Ethylendiaminotetraacetat interferiert bei der Eiweissbestimmung nach der Methode vonLowry, da sie selbst zur Reduktion des Folin-Reagens führt. Es gelingt, diese Interferenz durch Zusatz von CaCl₂ zu verhindern.     

The presence of specific proteins,in the absence of many serum proteins,in the rat seminiferous tubule fluid

Zusammenfassung Die Flüssigkeit in den Hodenkanälchen enthielt mehrere Proteine, die im Serum oder in der Hodenlymphe nicht nachweislich waren. Nur von einigen der Serumproteine waren in der Flüssigkeit der Hodenkanälchen schwache elektrophoretische Bänder zu sehen.

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Supported by a grant from the National Research Council for Medical Sciences, Helsinki, Finland.

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On sabbatical leave from the Department of Human Anatomy, School of Medicine, University of California, Davis (California 95616, USA).