文献类型：期刊文献

英文题名：Purification, Characterization, cDNA Cloning, and Bioinformatic Analysis of Zinc-Binding Protein from Magallana hongkongensis

作者：Chen, Citing[1];Li, Wan[1];Gao, Jialong[1,2];Cao, Wenhong[1,2];Qin, Xiaoming[1,2];Zheng, Huina[1,2];Lin, Haisheng[1,2];Chen, Zhongqin[1,2]

机构：[1]Guangdong Ocean Univ, Coll Food Sci & Technol, Zhanjiang 524088, Peoples R China;[2]Key Lab Adv Proc Aquat Prod Guangdong Higher Educ, Guangdong Prov Key Lab Aquat Prod Proc & Safety, Guangdong Prov Engn Lab Marine Biol Prod, Zhanjiang 524088, Peoples R China

年份：2024

卷号：29

期号：4

外文期刊名：MOLECULES

收录：SCI-EXPANDED(收录号：WOS:001175216900001)、、WOS

基金：No Statement Available

语种：英文

外文关键词：Magallana hongkongensis; zinc-binding protein; cDNA cloning; carbonic anhydrase

外文摘要：Oysters contain significant amounts of the zinc element, which may also be found in their proteins. In this study, a novel zinc-binding protein was purified from the mantle of the oyster Magallana hongkongensis using two kinds of gel filtration chromatograms. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) showed that its molecular weight was approximately 36 kDa. The protein identified by the Q-Exactive mass spectrometer shared the highest sequence identity with carbonic anhydrase derived from Crassostrea gigas concerning amino acid sequence similarity. Based on homologous cloning and RACE PCR, the full-length cDNA of carbonic anhydrase from Magallana hongkongensis (designated as MhCA) was cloned and sequenced. The cDNA of MhCA encodes a 315-amino-acid protein with 89.74% homology to carbonic anhydrase derived from Crassostrea gigas. Molecular docking revealed that the two zinc ions primarily form coordination bonds with histidine residues in the MhCA protein. These results strongly suggest that MhCA is a novel zinc-binding protein in Magallana hongkongensis.