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Citation: WANG Xing-Ming, DING Li-Sheng. The Reaction Mechanism Between Bacillus Subtilis Proteinase and Sodium 3,4-Dihydro-2-anthraquinone sulfonate[J]. Chinese Journal of Applied Chemistry, ;2004, 21(5): 459-463. shu

The Reaction Mechanism Between Bacillus Subtilis Proteinase and Sodium 3,4-Dihydro-2-anthraquinone sulfonate

WANG Xing-Ming ^a,, ,
DING Li-Sheng ^b

1.
a Department of Chemistry and Biology Engineering, Southwest University of Science and Technology, Mianyang 621002;
2.
b Chengdu Institute of Biology, Chinese Academy of Sciences, Chengdu

Corresponding author: WANG Xing-Ming,
Received Date: 25 April 2003
Available Online: 25 December 2003
Fund Project: 四川省教育厅自然科学基金重点资助项目(2000A56) (2000A56)

The interaction of bacillus subtilis proteinase(BSP) and sodium 3,4-dihydro-2-anthraquinone sulfonate(Alizarin Red S, ARS) was investigated by spectrophotometric method in acidic solution(pH=4.20). The red color of the solution indicates the formation of the new compound. The maximum absorption peak of the colored species was at 515 nm. It is shifted from 420 nm of ARS. Balance dialysis method, molar ratio method and double wavelengh method were adopted to investigate the association formation. The following results were obtained:binding number n₁=13, n₁=45; apparent molar absorptivity ε_B1=5.89×10³ L/(mol·cm), ε_B2=4.68×10³ L/(mol·cm); accumulative equilibrium constant β₁=5.27×10⁴ L/mol, β₂=3.54×10⁵ L/mol. It is found that combination of BSP with ARS conforms to Scatchard model and the first type binding number completely conform to functional atom number of BSP activity center in its space conformation. It is suggested that the combination between BSP and ARS is due to the electrostatic force(primary action force) and hydrophobic force.
- bacillus subtilis proteinase,
- sodium dihydro-anthraquinone sulfonate,
- accumulative equilibrium constant
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