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A novel and sensitive functional assay for complement Factor I based on the third proteolytic clip of C3b.
J Immunol Methods
June 2018
Department of Veterinary Medicine, University of Cambridge, UK.
A sensitive assay for the functional activity of complement Factor I is described. This is based on its third proteolytic clip whereby Factor I cleaves cell-bound iC3b to cell-bound C3dg and soluble C3c, thereby abolishing conglutination of the cells. Factor H is required as a co-factor for Factor I activity.
View Article and Find Full Text PDFDecolorization of dye solutions with Ruditapes philippinarum conglutination mud and the isolated bacteria.
J Environ Sci (China)
June 2011
Key Laboratory of Environmental Science and Technology, Education Department of Liaoning Province; School of Environmental and Chemical Engineering, Dalian Jiaotong University, Dalian 116028, China.
Application of Ruditapes Philippinarum conglutination mud (RPM) for decolorizing synthetic dye solutions was studied. RPM showed good activity for decolorization of Methylene Blue, Crystal Violet, Malachite Green, and Ink Blue. The amount of the RPM had great effect on the decoloration rate of the dye solutions.
View Article and Find Full Text PDFComparison between enzyme-linked immunosorbent assay, indirect fluorescent antibody and rapid conglutination tests in detecting antibodies against Babesia bovis.
Vet Parasitol
January 1998
Universidade para o Desenvolvimento do Estado e da Região do Pantanal, Brazil.
The performance of an enzyme-linked immunosorbent assay (ELISA), an indirect fluorescent antibody test (IFAT) and a rapid conglutination test (RCT) for the detection of antibodies against Babesia bovis, was evaluated with 462 cattle sera from Bahia State; Brazil. The results showed a concordance of 96.6% between the ELISA and IFAT, 90.
View Article and Find Full Text PDFStructure of a truncated human surfactant protein D is less effective in agglutinating bacteria than the native structure and fails to inhibit haemagglutination by influenza A virus.
Biochem J
April 1997
Department of Pathology, Osaka Prefectural Institute of Public Health, 1-3-69 Nakamichi, Higashinari, Osaka 537, Japan.
Surfactant protein D (SP-D) is a lung-specific protein that is synthesized and secreted by lung epithelial cells and is believed to play an important role in lung host defence. This protein belongs to the C-type lectin family, which is characterized by an N-terminal cysteine-rich domain, a collagen-like domain, a neck domain and a carbohydrate recognition domain (CRD). To elucidate the biological actions of this animal lectin against such pathogens as micro-organisms, the biological activities of a recombinant partial SP-D lacking a collagen-like domain were examined.
View Article and Find Full Text PDFConglutinin is a bovine serum protein which was first described as a vertebrate lectin. This protein belongs to the family of C-type lectins. These lectins are composed of four characteristic domains: (1) an N-terminal cysteine-rich domain, (2) a collagen-like domain, (3) a neck domain and (4) a carbohydrate recognition domain (CRD).
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