The self-thinning exponent in overcrowded stands of the mangrove, Kandelia obovata, on Okinawa Island, Japan

AbstractAutism spectrum disorder (ASD) subjects can present temporary behaviors of acute agitation and aggressiveness, named problem behaviors. They have been shown to be consistent with the self-organized criticality (SOC), a model wherein occasionally occurring “catastrophic events” are necessary in order to maintain a self-organized “critical equilibrium.” The SOC can represent the psychopathology network structures and additionally suggests that they can be considered as self-organized systems.

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The Nature of Rapidly Extracted Phycocyanin from the Blue-Green Alga Plectonema Boryanum

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100065870 ◽

1971 ◽

Vol 29 ◽

pp. 366-367

Author(s):

M. Kessel ◽

R. MacColl

Keyword(s):

Self Assembly ◽

Analytical Ultracentrifugation ◽

Uranyl Acetate ◽

The Self ◽

Major Protein ◽

Subunit Structure ◽

Blue Green Alga ◽

Thin Sections ◽

Blue Green Algae ◽

Cacodylate Buffer

The major protein of the blue-green algae is the biliprotein, C-phycocyanin (Amax = 620 nm), which is presumed to exist in the cell in the form of distinct aggregates called phycobilisomes. The self-assembly of C-phycocyanin from monomer to hexamer has been extensively studied, but the proposed next step in the assembly of a phycobilisome, the formation of 19s subunits, is completely unknown. We have used electron microscopy and analytical ultracentrifugation in combination with a method for rapid and gentle extraction of phycocyanin to study its subunit structure and assembly.To establish the existence of phycobilisomes, cells of P. boryanum in the log phase of growth, growing at a light intensity of 200 foot candles, were fixed in 2% glutaraldehyde in 0.1M cacodylate buffer, pH 7.0, for 3 hours at 4°C. The cells were post-fixed in 1% OsO4 in the same buffer overnight. Material was stained for 1 hour in uranyl acetate (1%), dehydrated and embedded in araldite and examined in thin sections.

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Interrelationship of the cellular distribution and secretion of regular structure (RS) protein in Bacillus licheniformis nm 105

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100123969 ◽

1992 ◽

Vol 50 (1) ◽

pp. 712-713

Author(s):

Xiaorong Zhu ◽

Richard McVeigh ◽

Bijan K. Ghosh

Keyword(s):

Alkaline Phosphatase ◽

Bacillus Licheniformis ◽

Self Assembly ◽

Gel Electrophoresis ◽

Culture Supernatant ◽

Regular Structure ◽

The Self ◽

Cellular Distribution ◽

Structural Protein ◽

Laboratory Cultures

A mutant of Bacillus licheniformis 749/C, NM 105 exhibits some notable properties, e.g., arrest of alkaline phosphatase secretion and overexpression and hypersecretion of RS protein. Although RS is known to be widely distributed in many microbes, it is rarely found, with a few exceptions, in laboratory cultures of microorganisms. RS protein is a structural protein and has the unusual properties to form aggregate. This characteristic may have been responsible for the self assembly of RS into regular tetragonal structures. Another uncommon characteristic of RS is that enhanced synthesis and secretion which occurs when the cells cease to grow. Assembled RS protein with a tetragonal structure is not seen inside cells at any stage of cell growth including cells in the stationary phase of growth. Gel electrophoresis of the culture supernatant shows a very large amount of RS protein in the stationary culture of the B. licheniformis. It seems, Therefore, that the RS protein is cotranslationally secreted and self assembled on the envelope surface.

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