收藏本站
收藏 | 手机打开
二维码
手机客户端打开本文

Purification and characterization of lizard fish pepsinogens and pepsins

Takeyuki Kanto  Kenji Hara  
【摘要】:正 Five pepsinogens were identified in lizard fish (Saurida wanieso) stomach and two of them (PG-Ⅰand PG-Ⅱ) were purified to homogeneity by column chromatographies on DEAE-Sephacel, Ultrogel AcA54, DEAE-Sepharose and Poly-L-Lysine Agarose. The molecular weights of the two purified PGs were about 41 kDa. Both pepsinogens were converted into pepsins within a few minutes under pH 2. 5. Corresponding pepsins were also purified by a chromatography on S-Sepharose and their molecular weights were 36 kDa as determined on SDS-PAGE. Optimum pHs of the pepsins were around 3. 5 and optimum temperatures were 45℃using hemoglobin as substrate. Both enzymes showed high sensitivity toward pepstatin A, a specific inhibitor of aspartic proteinases. The N-terminal amino acid sequences of PG-Ⅰand PG-Ⅱas determined to the 16th residue were exactly the same and showed high identity to pepsinogens of other animals.

知网文化
 快捷付款方式  订购知网充值卡  订购热线  帮助中心
  • 400-819-9993
  • 010-62982499
  • 010-62783978