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  • 1
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    Regulatory Peptides 29 (1990), S. 257-266 
    ISSN: 0167-0115
    Keywords: Adipose tissue ; Insulin ; Lipolytic activity ; Rabbit
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Medicine
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1432-1440
    Keywords: Diabetes mellitus ; Enteral formula ; Fructose ; Insulin ; Xylitol
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary To verify the benofit of nonglucose carbohydrates and fiber in enteral formula diets we studied the postprandial metabolism of eight healthy subjects after the intake of two helpings (25 g carbohydrates each) of five commonly used enteral formulas over 4 h. There were no significant differences in postprandial concentrations of blood glucose among the formulas. The area under the curve of postprandial insulin values, however, was significantly smaller after consumption of the fructose-containing formula (1948±285 μU min ml−1, P〈0.05) than after fiber-free (3222 ±678 μU min ml−1) or two fiber-containing products (2664±326 μU min ml−1, P〈0.05; and 3040±708 μU min ml−1, P〈0.05). The insulin area of the xylitol-containing formula (2307±364 μU min ml−1) was significantly smaller compared to the fiber-free product (P〈0.05). In addition, we found the postprandial increase in triglycerides to be significantly higher after the xylitol-containing formula (from 0.93±0.14 to 1.25±0.22 mmol/1) than after the fiber-free product (from 0.82±0.13 to 0.97±0.16 mmol/1, P〈0.05) or the two fiber-containing products (from 0.88±0.16 to 0.96±0.18 mmol/1, P〈0.05; and from 0.80±0.08 to 0.95±0.10 mmol/l, P〈0.05). We conclude that a patient with type 11 diabetes may benefit from replacing glucose and glucose-equivalent carbohydrates with fructose or xylitol.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Clinical and experimental medicine 147 (1968), S. 246-252 
    ISSN: 1591-9528
    Keywords: Lipolysis ; Fraction H ; Pituitary ; Purification ; Lipolyse ; Fraktion H ; Hypophyse ; Reinigung
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Description / Table of Contents: Zusammenfassung Es wird über die Gewinnung und weitere säulenchromatographische Reinigung einer lipolytisch wirksamen Substanz aus Schweinehypophysen (Fraktion H) berichtet. Auf Grund der untersuchten physikalisch-chemischen Eigenschaften kann gesagt werden, daß diese Substanz mit der vonRudman et al. extrahierten Fraktion H identisch ist. Durch Chromatographie an Sephadex G 50 konnte die Fraktion weiter gereinigt werden; die lipolytische Aktivität pro Gewichtseinheit wurde dadurch von 0,3 Μg auf 0,1 Μg in vitro bzw. von 125 Μg auf 63 Μg in vivo als minimal wirksame Dosen gesteigert, wie Untersuchungen an Meerschweinchen und Kaninchen ergaben. Eine Kontamination mit lipolytisch wirksamen Mengen ACTH wurde durch säulenehromatographische Untersuchungen auf Sephadex G 50 weitgehend ausgeschlossen.
    Notes: Summary The extraction and further purification of a lipolytic substance from hog pituitaries (Fraction H) are reported. This substance has physico-chemical properties identical with Fraction H extracted from pituitaries of pigs byRudman et al. Further purification was achieved by Sephadex-chromatographie. The lipolytic activity in the rabbit was augmented in vitro to 0.1 Μg/ml and in vivo to 63 Μg as minimal effective dose. A contamination with ACTH could be excluded by chromatography on Sephadex G 50.
    Type of Medium: Electronic Resource
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  • 4
    ISSN: 1432-0878
    Keywords: Lipolytic peptide B ; Pituitary ; ACTH/MSH cells ; Brain ; Immunocytochemistry
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Several lipid-mobilizing peptides occur in the pituitary, among them β-lipotropin and “lipolytic peptide A and peptide B”. The latter two peptides are distinct from β-lipotropin and appear to be chemically related to the neurophysins. Immunohistochemistry has now revealed that the lipolytic peptide B of the pituitary is localized in the ACTH- and MSH-cells. In addition, immunoreactive peptide B was found in axons of the posterior lobe of the pituitary. Immunoreactive peptide B was found also in nerve fibers and nerve cell bodies in the hypothalamus, particularly in the hypothalamo-hypophyseal tract and in the magnocellular neuronal system. Immunoreactive nerve fibers were numerous also in the periventricular nucleus of the thalamus. The antiserum against peptide B cross-reacts with neurophysin I, and hence, it cannot be excluded that at least part of the immunostaining in the brain reflects the presence of the latter component. However, the regional distribution of immunoreactive peptide B and neurophysin was not identical. Therefore, it is possible that authentic peptide B occurs not only in the pituitary but also in the brain.
    Type of Medium: Electronic Resource
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