Purification and characterization of &#x03B1;<inf>2</inf>-macroglobulin from chum salmon plasma

Abstract

Chum salmon plasma 2 -macroglobulin ( 2 -M) was first puri ed by polyethylene glycol gradient precipitation, gel ltration and anion-exchange chromatography from chum salmon plasma. The 2 -M was purified 47.77-fold with a yield of 28.90% towards papain. The 2 -M showed molecualr weight (Mw) of 175 kDa and consists of two different subunits of Mw 95 kDa and 80 kDa, respectively. The 2 -M was stable towards papain and trypsin at pH ranges from 5.0 to 8.0, and was thermal stable at temperatures below 50 . The 2 -M was applied to Alaska pollock surimi and was able to inhibit the gel weakening in a concentration-dependent manner.