Protein-hydrocarbon interactions. Interactions of various proteins with pure decane.
1. Solutions of a number of proteins were subjected to gentle agitation in the presence of small quantities of decane. 2. Some of the protein was lost from solution and adsorbed on the surface of the emulsion formed; at the same time some of the decane was bound to the protein remaining in solution. 3. The two processes were found to be related and a mechanism is proposed to explain the relationship. 4. With lysozyme and ribonuclease, the protein in the aqueous phase of an emulsion exhibited normal enzymic activity, whereas the fraction adsorbed on the interface was much less active but recovered activity on desorption.
D000327:Adsorption; D000473:Alkanes; D000818:Animals; D002247:Carbon Isotopes; D002256:Carbonic Anhydrases; D002417:Cattle; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D004655:Emulsions; D005969:Glutamate Dehydrogenase; D007328:Insulin; D007700:Kinetics; D008837:Micrococcus; D009113:Muramidase / Q000032:analysis; D011485:Protein Binding; D011506:Proteins; D012260:Ribonucleases / Q000032:analysis; D012710:Serum Albumin, Bovine; D013499:Surface Properties; D014316:Tritium; D014465:Ultrasonics; D014732:Vibration
D000473:Alkanes; D002247:Carbon Isotopes; D004655:Emulsions; D007328:Insulin; D011506:Proteins; D014316:Tritium; D012710:Serum Albumin, Bovine; D005969:Glutamate Dehydrogenase; D012260:Ribonucleases; D009113:Muramidase; D002256:Carbonic Anhydrases