Dextran-gel filtration of enzymes in the presence of their high-molecular-weight substrates.
1. Trypsin and ribonuclease were filtered through dextran gel (Sephadex G-100) columns in the absence and presence of their respective substrates. In the presence of their high-molecular-weight substrates the enzymes emerged earlier from the columns. This appeared to be due to the reversible formation of specific enzyme-substrate complexes. 2. The possibility of separation of an enzyme from other proteins with similar molecular weights was demonstrated with trypsin and cytochrome c in the presence of casein.
D002364:Caseins; D002850:Chromatography, Gel; D003580:Cytochromes; D003911:Dextrans; D066298:In Vitro Techniques; D012343:RNA, Transfer; D012260:Ribonucleases; D014357:Trypsin
D002364:Caseins; D003580:Cytochromes; D003911:Dextrans; D012343:RNA, Transfer; D012260:Ribonucleases; D014357:Trypsin