|Effect of microbubble and its generation process on mixed liquor properties of activated sludge using Shirasu porous glass (SPG) membrane system.|
Chun Liu,Hiroshi Tanaka,Jin Ma,Lei Zhang,Jing Zhang,Xia Huang,Yoshiaki Matsuzawa
Microbubble aeration is supposed to be able to provide potential advantage for aerobic biological wastewater treatment due to enhancement of oxygen mass transfer. On the other hand, microbubble and its generation methods might affect mixed liquor properties of activated sludge. Then SPG membrane microbubble generation system was used to investigate variation of mixed liquor properties of activated sludge in microbubble aeration. The results indicated that sludge floatation happened in microbubble aeration due to attachment of microbubbles to sludge flocs, resulting in a decrease in mixed liquor suspended solid (MLSS) concentration and poor sludge settleability. The strong shear stress caused by liquid circulation pump during microbubble generation led to sludge broken, resulting in decreased sludge floc size and sludge organics release, such as extracellular polymers (EPS). The organics release from broken sludge flocs was the main reason for increased both supernatant organic content (especially organic colloids) and consequent supernatant turbidity. The re-flocculation ability of broken sludge flocs also depended on sludge EPS release. In addition, the viscosity of mixed liquor increased along with sludge broken and increased supernatant organic content but the surface tension of mixed liquor remained constant. These results displayed the possible problems to apply microbubble aeration in aerobic wastewater treatment processes based on activated sludge.
|Identification and quantification of Gi-type GTP-binding proteins that copurify with a pituitary somatostatin receptor.|
Luthin, D R, et al.
J. Biol. Chem., 268: 5990-6 (1993)
Somatostatin (SRIF) receptors of GH4C1 cells occupied with biotinyl-NH-[Leu8,D-Trp22,Tyr25] somatostatin28 (bio-S28) have been affinity purified over streptavidin affinity columns (Eppler, C. M., Zysk, J. R., Corbett, M., and Shieh, H.-M. (1992) J. Biol. Chem. 267, 15603-15612). This procedure results in the copurification of a single subtype of SRIF receptor (SSTR2) and associated guanine nucleotide-binding proteins (G proteins) that are coupled to these receptors. For accurate quantification it was necessary to: (i) use homogenous recombinant standards; (ii) accurately assess the purity of standards; (iii) determine recovery of G proteins during sample preparation and Western blotting; and (iv) account for cross-reactivity among antisera. Four pertussis toxin-sensitive G proteins were quantified with previously characterized polyclonal antisera. Gi alpha 1 also was measured with a novel, more sensitive monoclonal antibody (7H7). Go alpha and Gi alpha 2 but not Gi alpha 1 and Gi alpha 3 were detected in membrane extracts prepared from GH4C1 cells. In contrast, the G proteins copurified with SSTR2 receptors were predominantly Gi alpha 2 (50% of total G protein) and Gi alpha 3 (36% of total G protein), whereas Go alpha and Gi alpha 1 were negligible. G beta subunits also were detected. Silver staining confirmed the absence of a 39-kDa protein, corresponding to the M(r) of Go alpha associated with purified SRIF receptor-G protein complexes. These data suggest that SRIF receptors selectively couple to two G proteins, one of which is sparsely expressed in GH4C1 cells; the data conform to the notion that SRIF receptors discriminate between similar pertussis toxin-sensitive G proteins.