Purification of the threonine-sensitive aspartokinase-homoserine dehydrogenase complex using chromatography on substituted Sepharose columns

Two new methods of debittering protein hydrolysates and a fraction of hydrolysates with exceptionally high content of essential amino acids

“…Hydrophobic interaction chromatography on alkylsubstituted sepharose derivatives of water-soluble protein is used to obtain a high degree of purification of biological material (Cuatrecases and Alfinsen, 1971;Blumberg et al, 1972;Hjertén, 1973;Hofstee, 1973;Broussard et al, 1976; Wilchek and Mirom, 1976). Since data in the literature indicated that hydrophobic peptides cause the bitter taste in protein hydrolysates, we tested the efficiency of some sepharose-substituted gels for debittering bitter-tasting protein hydrolysates.…”

Chromatography of Antihemophilic Factor on Diaminoalkane- and Aminoalkane-Derivatized Sepharose

“…Figs. 3-5 shows that binding of protein and WII: C depends primarily on the chain length of the ligand attached to the Sepharose beads; similar results have been obtained with various enzymes (24,25). The presence or absence of an amino end-group, or even substitution of the hydrogen atoms with bulky ethyl groups, have less influence.…”

Studies on the Plastein Formation and Enzymatic Protein Hydrolysates

“…Hydrophobic interaction chromatography on alkyl-substituted sepharose derivatives of water-soluble protein is used to obtain a high degree of purification of biological material, Cuatrecases and Alfinsen (1971), Blumberg et al (1972), Hjertén (1973), Hofstee (1973), Broussard et al (1976), wS'lchek and Mirom (1976. Since data in the literature indicated that hydrophobic peptides cause the bitter taste in protein hydrolysates, we tested the efficiency of some sepharose-substituted gels for debittering bitter tasting protein hydrolysates.…”