Gliocladium catenulatum in Association with Sclerotium cepivorum on Onion Leaves in Ghana.
During regular surveys of disease in farmers’ fields onion (Allium cepa L.) in the Upper East Region of Ghana in March 1997, white rot disease infected bulbs were collected for identification. Most of the white mycelium present on a scale of onions were cultured on potato dextrose agar (PDA). After 2 days of incubation, a white fluffy mycelium is observed later developed black sclerotia on the surface of the colonies to confirm the identity of Sclerotium cepivorum.
Ten days later, unknown fungus was observed to grow from the original inoculation point of S. cepivorum mycelium. pure culture of fungi known to grow on PDA sent to CAB International, UK, and was identified as a Gliocladium catenulatum Gilman and Abbott (1). G. catenulatum grow throughout the mycelia S. cepivorum and completely suppressed growth.
In culture, G. catenulatum colonized sclerotia of S. cepivorum and make them soft and easy to destroy, while sclerotia uncolonized remain resolute and difficult to destroy. The sclerotia uncolonized when transferred to the PDA produces a distinctive fluffy white mycelial growth of S. cepivorum; The colonized did not grow at all. G. catenulatum also reduce the growth of colonies, sclerotia formation and maturation of S. cepivorum. S. cepivorum culture inoculated with G. catenulatum measured 3 cm after 3 days of incubation and rarely exhibited mycelial growth, while the culture of S. cepivorum 5 cm in diameter measured after 3 days of incubation and generate enough even a piece of abundant, fluffy mycelium growth.
Sclerotia produced profusely in pure culture of S. cepivorum while that of G. catenulatum and S. cepivorum in combination produced only two sclerotia after 6 days and is then colonized by G. catenulatum. Striking characteristics of G. catenulatum is the production of yellow pigmentation around the margins of the colony. Species in the genus Gliocladium known to conflict with, and parasites on, other fungi. Antagonist properties and / or parasites of G. catenulatum in S. cepivorum indicate a possible role in biological control. This is the first report of G. catenulatum in association with S. cepivorum the shallots in Ghana.
Gliocladium catenulatum in Association with Sclerotium cepivorum on Onion Leaves in Ghana.
biologies utopian.
In 1924, British biologist J.B.S. Haldane admitted that anyone who tries to predict where science we are obligated to H.G. Wells, because ‘[t] he very mention of the future showed him’. However, Haldane complained that Wells was a ‘generation behind the times’, which has been raised when flying and radiotelegraphy is a question really scientific, but they are now only’ commercial issues, Haldane asserted, and “I believe that the center of scientific interest lies in biology ‘.
Haldane belief that biology is the key to the future too much is given, and lies in the background of the two books. Helen Curry researching the early history of dream engineering new types of plant, using the first X-ray, then colchicine (a chemical mutagen), and then a new source of intense radioactivity created by the nuclear reactor start.
Description: Adiponectin is an adipose-derived secreted protein that influences the body’s response to insulin. Adiponectin belongs to the soluble defence collagen super family and is involved with the promotion of adipocyte differentiation, fatty acid catabolism, and insulin resistance. Recombinant adiponectin is a multimeric glycoprotein that also has anti-inflammatory effects on the cell lining of blood vessel walls. High blood levels of adiponectin are associated with reduced risks of heart attacks while low levels are associated with obesity and an increased risk of heart attacks.
Description: Adiponectin is an adipose-derived secreted protein that influences the body’s response to insulin. Adiponectin belongs to the soluble defence collagen super family and is involved with the promotion of adipocyte differentiation, fatty acid catabolism, and insulin resistance. Recombinant adiponectin is a multimeric glycoprotein that also has anti-inflammatory effects on the cell lining of blood vessel walls. High blood levels of adiponectin are associated with reduced risks of heart attacks while low levels are associated with obesity and an increased risk of heart attacks.
Description: Adiponectin is an adipose-derived secreted protein that influences the body’s response to insulin. Adiponectin belongs to the soluble defence collagen super family and is involved with the promotion of adipocyte differentiation, fatty acid catabolism, and insulin resistance. Recombinant adiponectin is a multimeric glycoprotein that also has anti-inflammatory effects on the cell lining of blood vessel walls. High blood levels of adiponectin are associated with reduced risks of heart attacks while low levels are associated with obesity and an increased risk of heart attacks.
Description: The Acrp30 Human protein contains 226 amino acids and having a molecular mass of 24.54 kDa. Native adiponectin is isolated from human pooled sera and contains all HMW, MMW and LMW fractions.
Description: Adiponectin, also known as Acrp30, is an adipocyte-derived protein with wide ranging paracrine and endocrine effects on metabolism and inflammation. It promotes adipocyte differentiation, fatty acid catabolism, and insulin sensitivity, and is negatively correlated with obesity, type 2 diabetes, and atherogenesis. In this context, adiponectin is an antiinflammatory agent, but it exerts proinflammatory effects in nonmetabolic disorders such as rheumatoid arthritis and inflammatory bowel disease. Adiponectin interacts with the receptors AdipoR1 and AdipoR2, calreticulin, and Cadherin13/ T-Cadherin, as well as with several growth factors. Mature mouse adiponectin consists of a 66 amino acid (aa) N-terminal collagenous region and a 137 aa C terminal C1q like globular domain which can be cleaved by a leukocytederived elastase. Mature mouse adiponectin shares 83% and 91% amino acid (aa) sequence identity with human and rat adiponectin, respectively. Adiponectin associates into trimers that may assemble into medium molecular weight (MMW) hexamers and then into >300 kDa high molecular weight (HMW) oligomers. The glycosylation of four hydroxylated lysine residues in the collagenous domain is required for the intracellular formation of HMW complexes. The various multimeric forms of adiponectin exhibit distinct tissue specific and gender specific profiles and activities.
Description: Adiponectin, also known as Adipocyte complement-related protein of 30 kDa (Acrp30), is secreted from adipocytes and has been implicated in energy homeostasis and obesity.
Description: Adiponectin is an adipose-derived secreted protein containing 226 amino acid residues. It is relatively abundant in humans and rodents, accounting for about 0.01% of total plasma protein. The circulating levels of adiponectin are decreased under conditions of obesity, insulin resistance, and type II diabetes. Disruption of adiponectin in mice causes insulin resistance and neointimal formation. Conversely, administration of recombinant adiponectin suppresses hepatic glucose production, and reverses insulin resistance associated with both lipoatrophy and obesity. The protective role of adiponectin is attributed to its anti-inflammatory properties (e.g. ability to suppress expression of TNF-α and class A scavenger receptor in macrophages). Recombinant adiponectin is a multimeric glycoprotein containing amino acids Glu-19 to Asn-244 of the adiponectin precursor protein fused to an N-terminal histidine tag. Monomeric glycosylated adiponectin migrates at an apparent molecular weight of approximately 35.0 kDa by SDS PAGE analysis under reducing conditions.
Description: Adiponectin is an adipose-derived secreted protein containing 226 amino acid residues. It is relatively abundant in humans and rodents, accounting for about 0.01% of total plasma protein. The circulating levels of adiponectin are decreased under conditions of obesity, insulin resistance, and type II diabetes. Disruption of adiponectin in mice causes insulin resistance and neointimal formation. Conversely, administration of recombinant adiponectin suppresses hepatic glucose production, and reverses insulin resistance associated with both lipoatrophy and obesity. The protective role of adiponectin is attributed to its anti-inflammatory properties (e.g. ability to suppress expression of TNF-α and class A scavenger receptor in macrophages). Recombinant adiponectin is a multimeric glycoprotein containing amino acids Glu-19 to Asn-244 of the adiponectin precursor protein fused to an N-terminal histidine tag. Monomeric glycosylated adiponectin migrates at an apparent molecular weight of approximately 35.0 kDa by SDS PAGE analysis under reducing conditions.
Description: Adiponectin is an adipose-derived secreted protein containing 236 amino acid residues. It is relatively abundant in humans and rodents, accounting for about 0.01% of total plasma protein. The circulating levels of adiponectin are decreased under conditions of obesity, insulin resistance, and type II diabetes. Disruption of adiponectin in mice causes insulin resistance and neointimal formation. Conversely, administration of recombinant adiponectin suppresses hepatic glucose production, and reverses insulin resistance associated with both lipoatrophy and obesity. The protective role of adiponectin is attributed to its anti-inflammatory properties (e.g. ability to suppress expression of TNF-beta and class A scavenger receptor in macrophages). Recombinant adiponectin is a multimeric glycoprotein containing amino acids Val-21 to Asn-247 of the adiponectin precursor protein fused to an N-terminal histidine tag. Monomeric glycosylated adiponectin migrates at an apparent molecular weight of approximately 35.0 kDa by SDS PAGE analysis under reducing conditions.
Description: Adiponectin is an adipose-derived secreted protein containing 236 amino acid residues. It is relatively abundant in humans and rodents, accounting for about 0.01% of total plasma protein. The circulating levels of adiponectin are decreased under conditions of obesity, insulin resistance, and type II diabetes. Disruption of adiponectin in mice causes insulin resistance and neointimal formation. Conversely, administration of recombinant adiponectin suppresses hepatic glucose production, and reverses insulin resistance associated with both lipoatrophy and obesity. The protective role of adiponectin is attributed to its anti-inflammatory properties (e.g. ability to suppress expression of TNF-beta and class A scavenger receptor in macrophages). Recombinant adiponectin is a multimeric glycoprotein containing amino acids Val-21 to Asn-247 of the adiponectin precursor protein fused to an N-terminal histidine tag. Monomeric glycosylated adiponectin migrates at an apparent molecular weight of approximately 35.0 kDa by SDS PAGE analysis under reducing conditions.
Description: ACRP30 Rat Recombinant produced in 293 cell line is a polypeptide chain containing 238 amino acids and having a total molecular mass of 25.7 kDa. ACRP30 contains a C-Terminal linker (3 AA residue) and a C-Terminal Flag- tag (8 AA residue).
Description: The Adiponectin Human recombinant protein is a single, non-glycosilated polypeptide chain produced in E. coli, having a molecular weight of 25.1 kDa and containing 231 amino acids (15-244).
Human Adiponectin (ACRP30) Deficient Plasma (Heparin)
Description: Acrp30 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 158 amino acids (108-244 a.a.) and having a molecular mass of 18.1kDa.;Acrp30 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Human Adiponectin (ACRP30) AssayLite Antibody (RPE Conjugate)
Description: Acrp30 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 146 amino acids (106-242a.a.) and having a molecular mass of 16.9kDa. (Molecular size on SDS-PAGE will appear at approximately 13.5-18kDa). Acrp30 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Description: The Acrp30 Human is created as a recombinant protein with N-terminal fusion of His Tag. The Adiponectin His-Tagged Fusion Protein, produced in E. coli, is 26.4 kDa protein containing 230 amino acid residues of the Acrp30 Human and 12 additional amino acid residues - HisTag (underlined).
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Instead, Ewa Luczak interested eugenics influence on American literature, with a focus mainly on Jack London, Charlotte Perkins Gilman and George Schuyler. What unites these books (and their diverse topics address) are new ways of imagining the future, especially the future that is based in biology.
