A restoration-promoting integrated floating bed and its experimental performance in eutrophication remediation.

Numerous studies on eutrophication remediation have mainly focused on purifying water first, then restoring submerged macrophytes. A restoration-promoting integrated floating bed (RPIFB) was designed to combine the processes of water purification and macrophyte restoration simultaneously. Two outdoor experiments were conducted to evaluate the ecological functions of the RPIFB. Trial 1 was conducted to compare the eutrophication purification among floating bed, gradual-submerging bed (GSB) and RPIFB technologies. The results illustrated that RPIFB has the best purification capacity. Removal efficiencies of RPIFB for TN, TP, NH(+)4-N, NO(-)3-N, CODCr, Chlorophyll-a and turbidity were 74.45%, 98.31%, 74.71%, 88.81%, 71.42%, 90.17% and 85%, respectively. In trial 2, influences of depth of GSB and photic area in RPIFB on biota were investigated. When the depth of GSB decreased and the photic area of RPIFB grew, the height of Potamogeton crispus Linn. increased, but the biomass of Canna indica Linn. was reduced. The mortalities of Misgurnus anguillicaudatus and Bellamya aeruginosa in each group were all less than 7%. All results indicated that when the RPIFB was embedded into the eutrophic water, the regime shift from phytoplankton-dominated to macrophyte-dominated state could be promoted. Thus, the RPIFB is a promising remediation technology for eutrophication and submerged macrophyte restoration.

Identification of nitroglycerin-induced cysteine modifications of pro-matrix metalloproteinase-9.

Nitroglycerin (NTG), an important cardiovascular agent, has been shown recently to activate matrix metalloproteinase-9 (MMP-9) in biological systems, possibly leading to destabilization of atherosclerotic plaques. The chemical mechanism for this activation, particularly on the cysteine switch of the pro-form of MMP-9 (proMMP-9), has not been investigated and was examined here using nano-flow liquid chromatography coupled to mass spectrometry. In order to obtain high sequence coverage, two orthogonal enzymes (trypsin and GluC) were employed to digest the protein in parallel. Two complementary activation methods, collision-induced dissociation (CID) and electron-transfer dissociation (ETD), were employed for the identification of various modifications. A high-resolution Orbitrap analyzer was used to enable confident identification. Incubation of NTG with proMMP-9 resulted in the formation of an unstable thionitrate intermediate and oxidation of the cysteine switch to sulfinic and irreversible sulfonic acid derivatives. The unstable thionitrate modification was confirmed by both CID and ETD in the proteolytic peptides produced by both trypsin and GluC. Incubation of proMMP-9 with diethylenetriamine NONOate (a nitric oxide donor) led to sulfonic acid formation, but no observable sulfinic acid modification. Extensive tyrosine nitration by NTG was observed at Tyr-262, in close proximity to an oxidized Cys-256 of proMMP-9. The intramolecular interaction between these two residues toward NTG-induced oxidation was examined using a synthesized peptide representing the sequence in this domain, PWCSTTANYDTDDR, and the modification status was compared against an analog in which Cys was substituted by Ala. We observed a thionitrate product, extensive Cys oxidative modifications and enhanced tyrosine nitration with the Cys peptide but not with the Ala analog. Our results indicated that neighboring Cys and Tyr residues can facilitate each other's oxidation in the presence of NTG.