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  • Biochemistry and Biotechnology  (3)
  • ELISA  (2)
  • 1
    Electronic Resource
    Electronic Resource
    Ocular vascular endothelial growth factor levels in diabetic rats are elevated before observable retinal proliferative changes (1997)
    Springer
    Diabetologia 40 (1997), S. 726-730 
    Details
    ISSN: 1432-0428
    Keywords: Keywords Vascular endothelial growth factor ; vascular permeability factor ; Goto-Kakisaki rat ; diabetic retinopathy ; ELISA ; immunohistochemistry.
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Vascular endothelial growth factor (VEGF) is a potent angiogenic factor. VEGF levels in ocular tissue of 6-, 12-, 18- and 28-week-old Goto-Kakizaki (GK) rats, a well-known model of non-insulin-dependent diabetes, were evaluated by highly sensitive ELISA. VEGF concentrations in the GK rat as well as in non-diabetic Wistar rat significantly decreased from the age of 6 weeks to 18 weeks. However, although VEGF concentrations in the Wistar rat continued to fall significantly from 18 to 28 weeks of age, the levels were maintained between 18 and 28 weeks of age in GK rats. Levels were significantly different between the GK and Wistar rats at 28 weeks of age. Results of immunohistochemical studies of the eyes of Wistar and GK rats at 28 weeks of age suggest diffuse distribution of this cytokine in cells of neural origin. Weak to moderate VEGF immunoreactivity was exhibited mainly in the ganglion cell layer, inner plexiform layer and inner/outer nuclear layers in rats with and without diabetes. However, in the retinal optic nerve fiber layer, retinal pigment epithelium and choroid, strong VEGF immunoreactivity was noted only in the GK rat. In conclusion, increased VEGF production in certain ocular tissue, similar to that in humans, is observed quite early, at least before the appearance of observable retinal changes in the diabetic GK rat. This also suggests that the GK rat can be used as a model of initial or latent phase diabetic retinopathy. [Diabetologia (1997) 40: 726–730]
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s001250050740
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  • 2
    Electronic Resource
    Electronic Resource
    Characterization of fibronectin metabolites in normal rat urine
    Amsterdam : Elsevier
    Biochimica et Biophysica Acta (BBA)/General Subjects 967 (1988), S. 176-182 
    Details
    ISSN: 0304-4165
    Keywords: (Rat urine) ; Characterization ; ELISA ; Fibronectin metabolite ; Immunoblotting
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Medicine , Physics
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0304-4165(88)90007-4
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  • 3
    Electronic Resource
    Electronic Resource
    Application of polylysine bound succinyl-NA to a membrane reactor (1976)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 18 (1976), S. 1761-1775 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: The amide bond at N-6 in succinyl-NAD was found to be more stable than in former accounts. Succinyl-NAD was coupled on polylysine to give a new polymer derivative of NAD, which retained at least 85% of the initial coenzymic activity even after dialysis for one week. The polymer derivative of NAD could be applied to a membrane reactor containing alcohol dehydrogenase and lactate dehydrogenase and lactate was continuously produced in a half-life of ten days.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260181210
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  • 4
    Electronic Resource
    Electronic Resource
    Preparation of immobilized enzymes from acrylic monomers under γ-ray irradiation (1975)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 17 (1975), S. 119-128 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Immobilized glucoamylase, invertase, and β-galactosidase were prepared by using 2-hydroxyethyl acrylate and dimethylacrylamide under γ-ray irradiation. In the case of 2-hydroxyethyl acrylate, the monomer-enzyme solution was changed to the gel by irradiation of less than 1.0 Mrad, but it was difficult to eliminate enzyme leakage from the gel. When leakage was eliminated by increased irradiation, the activities of the gels were very low. In the case of dimethylacrylamide, the monomer-enzyme solution was changed to a gel by irradiation of 1.0 Mrad; leakage could be eliminated by irradiation of 2.0 Mrad. This gel possessed very high activity. In the case of acrylic acid-sodium acrylate, the monomer-enzyme solution could not be changed to a gel. In preparing gels, high concentrations of enzyme protein had a tendency to obstruct gelation.
    Additional Material: 4 Tab.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260170110
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  • 5
    Electronic Resource
    Electronic Resource
    Preparation of immobilized enzymes by N-Vinylpyrrolidone and the general properties of the glucoamylase gel (1974)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 16 (1974), S. 1517-1528 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Immobilized glucoamylase, invertase, and β-galactosidase were prepared by using N-vinylpyrrolidone monomer (VP) under γ-ray irradiation. The enzyme-VP solutions were gelled by irradiation with 2.9 Mrad and the added enzymes were almost completely entrapped. Activity losses on entrapping were 55% for the VP-glucoamylase gel, and more than 90% in the case of VP-invertase and VP-β-galactosidase gels. No leakage of enzyme from these gels could be detected within 1 hr. The VP-glucoamylase gel was capable of hydrolyzing dextrin (mol wt 10,400) to glucose and the glucose equivalent was equal to that obtain able with native enzyme. The optimum temperature, heat stability, pH activity curve, and pH stability of VP-glucoamylase gel were slightly inferior to those of native enzyme, while Km was a little larger than that of native enzyme.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260161108
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