Rye germ acid phosphatase: properties of the enzyme and its activation by lectins |
| |
| Authors: | Mirosława Ferens Bronisława Morawiecka |
| |
| Affiliation: | Institute of Biochemistry, University of Wroc?aw, Poland |
| |
| Abstract: | Acid phosphatase (EC 3.1.3.2) from rye germs is a glycoprotein of M, 90000 with subunit structure. The pH optimum for pNPP hydrolysis is 5.4. The best substrates for the enzyme are pNPP, PPi and ATP. In the presence of plant lectins an increase in AcPase activity was found. ConA causes a 20% decrease of Kmapp and a 50% increase of Vmaxapp with pNPP as substrate. |
| |
| Keywords: | Gramineae rye germ acid phosphatase lectin ConA. AcPase, acid phosphatase FDP, fructose 1,6-biphosphate PAGE, polyacrylamide gel electrophoresis ConA, concanavalin A LL, lentil lectin SBA, soybean agglutinin WGA, wheat germ agglutinin RGA, rye germ agglutinin. |
| 本文献已被 ScienceDirect 等数据库收录！ |
|
