Abstract: The vitellin was purified from eggs of the locust Catantops pinguis (Stål) using distilled water precipitation, gel filtration and gel electrophoresis. Its properties were also analyzed using polyacrylamide gel electrophoresis and different dyeing methods. The results indicated that the vitellin of C. pinguis was a kind of protein containing sugar and fat. The molecular weight of the vitellin was 548 kD, consisting of seven subunits with molecular weight of 147.3, 100.2, 95.9, 59.6, 53.6, 49.0 and 42.2 kD, respectively. From the vitellin, 17 kinds of amino acids and NH₃ peaks were detected by HPLC, among which the content of Glu was highest with 13.46% in the vitellin, and the contents of Asp, Leu, Cys and Arg were relatively high, while contents of Pro, His and Lys were low.

Key words: Catantops pinguis, vitellin, purification, property