Expression of a bee venom phospholipase A2 from Apis cerana cerana in the baculovirus-insect cell.

ABSTRACT: Bee venom phospholipase A(2) (BvPLA(2)) is a lipolytic enzyme that catalyzes the hydrolysis of the sn-2 acyl bond of glycerophospholipids to liberate free fatty acids and lysophospholipids. In this work, a new BvPLA(2) (AccPLA(2)) gene from the Chinese honeybee (Apis cerana cerana) venom glands was inserted into bacmid to construct a recombinant transfer vector. Tn-5B-4 (Tn) cells were transfected with the recombinant bacmid DNA for expression. Sodium dodecylsulfate-polyacrylamide gel electrophoresis (SDS-PAGE) analysis revealed a double band with molecular weights of 16 and 18 kDa. Products of hexahistidine AccPLA(2) fusion protein accumulated up to 5.32% of the total cellular proteins. The AccPLA(2) fusion protein was cross reactive with the anti-AmPLA(2) (BvPLA(2) of the European honeyb

SUBMITTER: Shen LR 

PROVIDER: S-EPMC2865836 | biostudies-literature | 2010 May

REPOSITORIES: biostudies-literature