Anti-algae efficacy of silver nanoparticles to Microcystis aeruginosa : Influence of NOM, divalent cations, and pH

Author(s):  
Tiandi Huang ◽  
Minghao Sui ◽  
Xin Yan ◽  
Xuan Zhang ◽  
Zhen Yuan
2009 ◽  
Vol 32 (3) ◽  
pp. 423-428 ◽  
Author(s):  
Myung-Hwan Park ◽  
Keun-Hee Kim ◽  
Huk-Hee Lee ◽  
Jin-Seog Kim ◽  
Soon-Jin Hwang

1961 ◽  
Vol 7 (6) ◽  
pp. 869-882 ◽  
Author(s):  
Jack McLachlan ◽  
P. R. Gorham

A dilute precipitate-free medium has been developed for the culture of Microcystis aeruginosa Kütz. With this medium, maximum growth rates of approximately 1.5 divisions per day have been attained during the first 3 days. Buffering between pH 7.4 and 7.7 with 10 mM tris (hydroxymethyl) aminomethane (TRIS) caused no toxicity. TRIS increased the tolerance of the alga towards supraoptimal concentrations of monovalent but not divalent cations. High concentrations of magnesium were toxic, but toxicity disappeared when magnesium: calcium ratios of 33:1 or lower were provided. An increase in nitrogen concentration caused no increase in yield, but a decrease caused a reduction. Doubling or halving the concentration of all other salts had no effect on yields. Growth in this medium was apparently limited by factors other than mineral nutrients. This alga has a rather low tolerance for potassium and requires little, if any, sodium.


Author(s):  
William J. Dougherty ◽  
Samuel S. Spicer

In recent years, considerable attention has focused on the morphological nature of the excitation-contraction coupling system of striated muscle. Since the study of Porter and Palade, it has become evident that the sarcoplastic reticulum (SR) and transverse tubules constitute the major elements of this system. The problem still exists, however, of determining the mechamisms by which the signal to interdigitate is presented to the thick and thin myofilaments. This problem appears to center on the movement of Ca++ions between myofilaments and SR. Recently, Philpott and Goldstein reported acid mucosubstance associated with the SR of fish branchial muscle using the colloidal thorium dioxide technique, and suggested that this material may serve to bind or release divalent cations such as Ca++. In the present study, Hale's iron solution adapted to electron microscopy was applied to formalin-fixed myofibrils isolated from glycerol-extracted rabbit psoas muscles and to frozen sections of formalin-fixed rat psoas muscles.


Author(s):  
N. Panté ◽  
M. Jarnik ◽  
E. Heitlinger ◽  
U. Aebi

The nuclear pore complex (NPC) is a ∼120 MD supramolecular machine implicated in nucleocytoplasmic transport, that is embedded in the double-membraned nuclear envelope (NE). The basic framework of the ∼120 nm diameter NPC consists of a 32 MD cytoplasmic ring, a 66 MD ‘plug-spoke’ assembly, and a 21 MD nuclear ring. The ‘central plug’ seen in en face views of the NPC reveals a rather variable appearance indicating that it is a dynamic structure. Projecting from the cytoplasmic ring are 8 short, twisted filaments (Fig. 1a), whereas the nuclear ring is topped with a ‘fishtrap’ made of 8 thin filaments that join distally to form a fragile, 30-50 nm distal diameter ring centered above the NPC proper (Fig. 1b). While the cytoplasmic filaments are sensitive to proteases, they as well as the nuclear fishtraps are resistant to RNase treatment. Removal of divalent cations destabilizes the distal rings and thereby opens the fishtraps, addition causes them to reform. Protruding from the tips of the radial spokes into perinuclear space are ‘knobs’ that might represent the large lumenal domain of gp210, a membrane-spanning glycoprotein (Fig. 1c) which, in turn, may play a topogenic role in membrane folding and/or act as a membrane-anchoring site for the NPC. The lectin wheat germ agglutinin (WGA) which is known to recognize the ‘nucleoporins’, a family of glycoproteins having O-linked N-acetyl-glucosamine, is found in two locations on the NPC (Fig. 1. d-f): (i) whereas the cytoplasmic filaments appear unlabelled (Fig. 1d&e), WGA-gold labels sites between the central plug and the cytoplasmic ring (Fig. le; i.e., at a radius of 25-35 nm), and (ii) it decorates the distal ring of the nuclear fishtraps (Fig. 1, d&f; arrowheads).


Sign in / Sign up

Export Citation Format

Share Document