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  • 1990-1994  (4)
  • Cats  (2)
  • Biochemistry and Biotechnology  (1)
  • Proliferative vitreoretinopathy  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Comparative clinical pathology 1 (1991), S. 217-219 
    ISSN: 1433-2981
    Keywords: Lectins ; Erythrocytes ; Cats
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Blood groups A, B and AB of cats (not related to human blood groups) are defined serologically with feline antisera. Five cats were blood typed and used in this study. Three cats were type B; two were type A. Two per cent suspensions of red blood cells (RBCs) from each cat were prepared and used in agglutination tests with 11 commercial lectins. Lectins are carbohydrate-binding proteins of non-immune origin. Most of these lectins agglutinated either all or none of the five samples of RBCs. However, wheat germ lectin (WGL) strongly agglutinated feline type B RBCs, but did not agglutinate type A RBCs. Thus WGL may be useful in feline blood typing, especially because the naturally occurring anti-B isoagglutinin is of low incidence and low titre.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Comparative clinical pathology 1 (1991), S. 196-199 
    ISSN: 1433-2981
    Keywords: Erythrocyte membrane glycolipids ; Thin layer chromatography ; Cats
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Erythrocyte membrane glycolipids from blood type A and type B cats were examined by thin layer chromatography. The results indicate that the major erythrocyte membrane glycolipid of type A cats is NeuGc-NeuGc-Galactose-Glucose-Ceramide ([NeuGc]2GD3), where NeuAc represents N-glycolyl-neuraminic acid. In contrast, the major erythrocyte membrane glycolipid of type B cats is NeuAc-NeuAc-Galactose-Glucose-Ceramide ([NeuAc]2GD3), where NeuAc represents N-acetylneuraminic acid. These major erythrocyte membrane glycolipids may be the blood group antigens for type A and type B cats, respectively. All type A cats may have enzymes to synthesise erythrocyte membrane glycolipids with terminal NeuAc, whereas type B cats may lack the gene for N-acetylneuraminic acid hydroxylase, the enzyme that converts NeuAc into NeuGc.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Cell & tissue research 267 (1992), S. 185-192 
    ISSN: 1432-0878
    Keywords: Retina ; Proliferative vitreoretinopathy ; Epiretinal membrane ; Fibronectin ; In situ hybridisation ; Immunohistochemistry ; Man
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The distribution of fibronectin mRNA and fibronectin in adult human retina and epiretinal membranes was investigated by in situ hybridisation and immunohistochemical techniques. The cells in normal adult retina contained little or no fibronectin mRNA and the retina only showed fibronectin immunoreactivity in retinal vessels. The cells in detached neuroretina did not contain fibronectin message but the vitreoretinal interface of the detached retina exhibited variable fibronectin immunoreactivity. Retinal glia, retinal pigment epithelium and fibroblast-like cells in membranes at the vitreoretinal juncture (epiretinal membranes) showed variable labelling with the fibronectin mRNA probe and all the membranes immunostained for fibronectin. No difference could be detected between membrane cell types in the intensity of labelling with the mRNA probe or for fibronectin immunoreactivity. The results indicate that cells in situ in attached and detached adult human retina do not produce fibronectin. Although fibronectin at the vitreoretinal juncture in retinal detachment is probably partly derived from plasma fibronectin resulting from breakdown of the blood-retinal barrier, ectopic retinal cells produce fibronectin and contribute to the glycoprotein in epiretinal membranes.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 44 (1994), S. 1235-1245 
    ISSN: 0006-3592
    Keywords: hybridoma ; monoclonal antibody ; temperature ; nucleotides ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: The specific monoclonal antibody productivity (qMab) of a murine hybridoma (CC9C10) increased with incubation temperature in the range 33°C to 39°C. qMab was constant at each temperature and was independent of the phase of culture. The qMab increased 97% at 39°C and decreased by 21% at 33°C compared with controls at 37°C. Specific rates of substrate (glucose and glutamine) utilization and byproduct (lactate and ammonia) formation also increased with temperature but the yield coefficient, YLac/Llc' was constant for 33°C to 39°C and YAmm/Gin was constant for 37°C to 39°C. YAmm/Gin at 33°C was lower than the control. Changes in specific nucleotide concentrations and ratios were monitored by analysis of intracellular nucleotide pools. The NTP ratio, (ATP + GTP)/(UTP + CTP), increased and the U-ratio (UTP/UDP-GNac) decreased during the course of each culture, whereas the adenylate energy charge, (ATP + 0.5ADP)/(ATP + ADP + AMP), remained relatively constant at a value 0.8. The relative content of UDP-/N acetyl galactosamine, UDP-N acetyl glucosamine, and NAD increased with incubation temperature, whereas the relative ATP content, SA(ATP + ADP + AMP)/SU (UTP + UDP-sugars) ratio, purine/pyrimidine, ATP/GTP, and U-ratio decreased at higher incubation temperatures. It is possible that these nucleotide parameters may have a regulatory role in the changes of qMab observed at the higher temperatures. © 1994 John Wiley & Sons, Inc.
    Additional Material: 11 Ill.
    Type of Medium: Electronic Resource
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