Electrophoretic titration curve in 6 M urea of the bovine eye lens protein α-crystallin

✍ Scribed by Piet J.M. Van Den Oetelaar; Herman J. Hoenders

• Book ID: 104144481
• Publisher: Elsevier Science
• Year: 1987
• Tongue: English
• Weight: 733 KB
• Volume: 411
• Category: Article
• ISSN: 1873-3778
• DOI: 10.1016/s0021-9673(00)94010-x

✦ Synopsis

Recently we reported on the separation of the subunits of the bovine eye lens protein a-crystallin by means of fast protein liquid ehromatography-chromatofocusing in concentrated ureal. We noted that the pH at which the CYAN and aAz subunits eluted from the column differed by 0.41 pH unit from their pZ as determined by isoelectric focusing in concentrated urea, whereas there was no difference for the aB1 chain and only a difference of -0.09 pH unit for the ORBS subunit. Similar observations were made by Bloemendal and Groenewoud2 using a soft-gel PBE-94 column. We suggested that the difference in behaviour of the aA and aB chains is caused by a difference in the net charge of the subunits near their isoelectric point.