作者: Bo Yeon Kim , Byung Rae Jin
DOI: 10.1016/J.ASPEN.2016.07.013
关键词: Enzyme 、 Biology 、 Acid phosphatase 、 Apis cerana 、 Western blot 、 Phosphatase 、 Recombinant DNA 、 Biochemistry 、 Antibody 、 Venom
摘要: Abstract Bee venom contains a variety of toxic components, including enzymes, peptides, and biogenic amines. An acid phosphatase Acph-1-like protein has been identified from Asiatic honeybee (Apis cerana) venom. However, no molecular information is currently available for phosphatases A. cerana In this study, an (AcVAP) was identified. The amino sequence analysis the predicted AcVAP revealed high identity with other bee phosphatases. anti-AcVAP antibody produced against recombinant (46-kDa) expressed in baculovirus-infected insect cells. Northern Western blot analyses showed that gland present as 46-kDa secreted enzymatic properties were determined using p-nitrophenyl phosphate (p-NPP) substrate exhibited highest activity at pH 4.8 45 °C. Taken together, our data demonstrated functions phosphatase.