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: 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: 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).
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: 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: Trimeric form of Adiponectin Human trimeric form was expressed in HEK293 cells. The cysteine 39 was replaced with Alanine (C39A) 9. hAd-C39A can only form a trimer, but not a hexamer or an HMW form.
Acrp30 Human, Adiponectin Human Recombinant Protein, His tag
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).
Acrp30 Mouse, Adiponectin Mouse Recombinant Protein, Trimeric form
Description: Trimeric form of Acrp30 Mouse was expressed in HEK293 cells.;The cysteine 39 was replaced with alanine (C39A) 9. mAd-C39A can only form trimer, but not hexamer or HMW form.
Acrp30 Mouse, Adiponectin Mouse Recombinant Protein, His Tag
Description: The Adiponectin Mouse is created as a recombinant protein with a 21 a.a N-terminal fusion of His Tag. The Adiponectin His-Tagged Fusion Protein, produced in E. coli, is a 27.2kDa protein containing 251 amino acid residues of the Acrp30 Mouse, 18-247 amino acids.
Recombinant Mouse Adiponectin/Acrp30/AdipoQ ((N-6His, E. coli)
Description: Adiponectin Human Recombinant HMW Rich produced in HEK cells is a single, glycosylated, polypeptide chain (19-244) containing a total of 226 amino acids, having a molecular mass of 24.6kDa (calculated). Human Acrp30 HMW Rich migrates on SDS-PAGE under non-reducing conditions at ~ 884 kDa.
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.
Description: A polyclonal antibody for detection of Acrp30 from Human, Mouse, Rat. This Acrp30 antibody is for WB , ELISA. It is affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogenand is unconjugated. The antibody is produced in rabbit by using as an immunogen synthesized peptide derived from the Internal region of human Acrp30
Description: A polyclonal antibody for detection of Acrp30 from Human, Mouse, Rat. This Acrp30 antibody is for WB , ELISA. It is affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogenand is unconjugated. The antibody is produced in rabbit by using as an immunogen synthesized peptide derived from the Internal region of human Acrp30
Description: A polyclonal antibody for detection of Acrp30 from Human, Mouse, Rat. This Acrp30 antibody is for WB , ELISA. It is affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogenand is unconjugated. The antibody is produced in rabbit by using as an immunogen synthesized peptide derived from the Internal region of human Acrp30
Description: The gAcrp30 variant is a naturally occurring globular protein, obtained by proteolytic processing of adiponectin. Adiponectin is produced and secreted exclusively by adipocytes, and is a relatively abundant plasma protein, accounting for up to 0.05% of total serum protein. Like Adiponectin, Acrp30 is capable of decreasing hyperglycemia and reversing insulin resistance. Additionally, gAcrp30 has been shown to be an important factor in promoting fat loss by signaling muscle to absorb and burn Free-Fatty Acids (FFAs). The signaling receptors for adiponectin and gAcrp30 have recently been identified and names AdipoR1 and AdipoR2. AdipoR2 is predominantly expressed in the liver. This naturally occurring variant of human gAcrp30/Adipolean is an 18.1 kDa protein, containing 14 amino acids extra at the N-terminus of human gAcrp30/Adipolean.
Description: The gAcrp30 variant is a naturally occurring globular protein, obtained by proteolytic processing of adiponectin. Adiponectin is produced and secreted exclusively by adipocytes, and is a relatively abundant plasma protein, accounting for up to 0.05% of total serum protein. Like Adiponectin, Acrp30 is capable of decreasing hyperglycemia and reversing insulin resistance. Additionally, gAcrp30 has been shown to be an important factor in promoting fat loss by signaling muscle to absorb and burn Free-Fatty Acids (FFAs). The signaling receptors for adiponectin and gAcrp30 have recently been identified and names AdipoR1 and AdipoR2. AdipoR2 is predominantly expressed in the liver. This naturally occurring variant of human gAcrp30/Adipolean is an 18.1 kDa protein, containing 14 amino acids extra at the N-terminus of human gAcrp30/Adipolean.
Description: gAcrp30 is a naturally occurring globular protein, obtained by proteolytic processing of adiponectin. Adiponectin is produced and secreted exclusively by adipocytes, and is a relatively abundant plasma protein, accounting for up to 0.05% of total serum protein. Like Adiponectin, gAcrp30 is capable of decreasing hyperglycemia and reversing insulin resistance. Additionally, gAcrp30 has been shown to be an important factor in promoting fat loss by signaling muscle to absorb and burn Free-Fatty Acids (FFAs). The signaling receptors for adiponectin and gAcrp30 have recently been identified and names AdipoR1 and AdipoR2. AdipoR2 is predominantly expressed in the liver. Recombinant human gAcrp30/Adipolean is a 16.6 kDa protein consisting of 145 amino acid residues.
Description: gAcrp30 is a naturally occurring globular protein, obtained by proteolytic processing of adiponectin. Adiponectin is produced and secreted exclusively by adipocytes, and is a relatively abundant plasma protein, accounting for up to 0.05% of total serum protein. Like Adiponectin, gAcrp30 is capable of decreasing hyperglycemia and reversing insulin resistance. Additionally, gAcrp30 has been shown to be an important factor in promoting fat loss by signaling muscle to absorb and burn Free-Fatty Acids (FFAs). The signaling receptors for adiponectin and gAcrp30 have recently been identified and names AdipoR1 and AdipoR2. AdipoR2 is predominantly expressed in the liver. Recombinant human gAcrp30/Adipolean is a 16.6 kDa protein consisting of 145 amino acid residues.
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.
