Psb27, a photosystem II assembly protein,enables quenching of excess light energy during its participation in the PSII lifecycle

Photosynthesis Research - Photosystem II (PSII), the enzyme responsible for oxidizing water into molecular oxygen, undergoes a complex lifecycle during which multiple assembly proteins transiently...     

A Large Scale Preparation op Peanut Agglutinin on a New Affinity Matrix

A simple and rapid method for the purification of Peanut Agglutinin by affinity chromatography on cross-linked arabinogalactan is described. Cross-linked arabinogalactan shows a high capacity for PNA. The lectin has been obtained to electrophore-tic purity and has a high hemagglutinating specific activity.     

Metabolically active antigen presenting cells are required for human T cell proliferation in response to the superantigen streptococcal M protein

Abstract M protein from type 5 group A streptococci has been identified as a member of the family of polyclonal T cell activators termed superantigens because it preferentially stimulates T cells bearing specific Vβ elements of the T cell receptor (TCR). In this study the molecular and cellular requirements for presentation of this protein to T cells were investigated. Only accessory cells (AC) expressing class II major histocompatibility complex (MHC) molecules were capable of supporting T cell activation in response to a 22 kDa fragment of M protein (pep M). Despite the need for class II elements, processing of pep M5 by the antigen-presenting cells (APC) was not required for T cell proliferation induced by pep M5. Fixation of APC by paraformaldehyde (PF) treatment impaired their ability to induce optimal T cell proliferation in response to pep M5 withouth significantly affecting interleukin (IL-2) production. In contrast, PF-fixation of cells from the B cell lymphoma line, Raji, did not affect their ability to present pep M5 to human T cells. Addition of rIL-1 and IL-6 to PF-treated APC restored pep M5-induced blastogenesis. Our data suggest that pep M5 directly associates with HLA class II molecules forming a complex that can induce IL-2 production but not optimal proliferation by T cells. Additional signals provided by the AC are required to trigger optimal T cell proliferation in response to this superantigen.     

Effectiveness of Biosorption-Assisted Microfiltration Process for Treatment of Domestic Wastewater

The efficiency of a biosorbent prepared from Eichhornia crassipes roots (ECR) was explored for the treatment of domestic sewage water in combination with low-cost ceramic microfiltration membrane. Batch sorption studies were conducted as a function of biosorbent dose, initial chemical oxygen demand (COD) loading, and temperature. Sorption equilibrium data of varying initial COD values (116–800 mg/L) indicated high potential of ECR for COD removal. Using 0.25 g/L of biosorbent dose, the equilibrium adsorption capacity was obtained as 2480 mg/g at 20°C for an initial COD loading of 800 mg/L. Microfiltration study was performed using ceramic membrane made from composition of α-alumina and clay. The effect of operating parameters on filtration characteristics was observed in terms of permeate flux. Permeate samples were characterized in terms of various parameters both for the direct filtration, as well as biosorbent-assisted filtration. The filtration behavior of wastewater at varying transmembrane pressure was explained using various membrane fouling models. The results suggested that microfiltration of domestic wastewater with incorporation of biosorbent (0.25 g/L) was highly effective for removal of organic load (>90%), turbidity (>99%), and total suspended solids (TSS) (93–95%) and the treated water quality was suitable for reuse in various purposes, such as gardening, floor and car washing, etc.     

Chemical modification of acetylcholinesterase from eel and basal ganglia: effect on the acetylcholinesterase and aryl acylamidase activities

The effect of chemical modification on the acetylcholinesterase and the aryl acylamidase activities of purified acetylcholinesterase from electric eel and basal ganglia was investigated in the presence and absence of acetylcholine, the substrate of acetylcholinesterase, and 1,5-bis[4-(allyldimethylammonium)phenyl]pentan-3-one dibromide (BW284C51), a reversible competitive inhibitor of acetylcholinesterase. Trinitrobenzenesulfonic acid, pyridoxal phosphate, acetic anhydride, diethyl pyrocarbonate, and 2-hydroxy-5-nitrobenzyl bromide under specified conditions inactivated both acetylcholinesterase and aryl acylamidase in the absence of acetylcholine and BW284C51. Chemical modifications in the presence of acetylcholine and BW284C51 by all the above except diethyl pyrocarbonate selectively prevented the loss of acetylcholinesterase but not aryl acylamidase activity; modification by diethyl pyrocarbonate in the presence of acetylcholine and BW284C51 prevented the loss of both acetylcholinesterase and aryl acylamidase activities. Treatment with N-acetylimidazole resulted in the inactivation of acetylcholinesterase and the activation of aryl acylamidase. These changes in both the activities could be prevented by acetylcholine and BW284C51. Modification by phenylglyoxal, 2,4-pentanedione, or N-ethylmaleimide did not affect the enzyme activities. Indophenylacetate hydrolase activity followed a pattern similar to that of acetylcholinesterase in all the above modification studies. The results suggested essential lysine, tyrosine, tryptophan, and histidine residues for the active center of acetylcholinesterase and essential lysine, histidine, and tryptophan residues for the active center of aryl acylamidase.(ABSTRACT TRUNCATED AT 250 WORDS)