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  • 1
    ISSN: 1432-0428
    Keywords: Type 2 diabetes ; very low-density lipoproteins ; dietary treatment
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary To evaluate possible influences of dietary intervention on the composition of very low-density lipoproteins (VLDL), ten subjects with Type 2 (non-insulin dependent) diabetes mellitus received a hypocaloric regimen. Fifteen healthy subjects served as controls. Ultracentrifuged VLDL were analysed as cholesterol, triglycerides, apolipoprotein B (apo B), and the soluble apolipoproteins C and E (polyacrylamide gel electrophoresis in urea and densitometry) before the study, after 2 weeks and then after 3 months. Compared with the control subjects, the content of cholesterol and apo E in the VLDL was elevated in the diabetic subjects, while the area ratio of apo C-II to apo C-III1 was lowered. After diet the reduction in VLDL was accompanied by compositional changes: a decrease of the cholesterol/triglyceride ratio and of the apo E/apo C area ratio. The apo C-II/apo C-III1 area ratio remained unaffected. We conclude that one beneficial effect of therapeutic intervention in diabetes may lie in lowering the level of possibly atherogenic VLDL-components.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Journal of molecular medicine 60 (1982), S. 637-649 
    ISSN: 1432-1440
    Keywords: Serum apolipoproteins ; Function ; Diet ; Drugs ; Atherosclerosis ; Apolipoproteine ; Einflüsse ; Ernährung ; Medikamente ; Krankheiten ; Artheriosklerose
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Description / Table of Contents: Zusammenfassung Im Humanserum sind bisher zwölf verschiedene Apolipoproteine nachgewiesen worden. Apo A–I and Apo A–II sind Strukturproteine der HDL und haben Coenzymfunktion für die LCAT. Apo B ist Hauptprotein der LDL, kommt aber auch in den triglyceridreichen Lipoproteinen vor und ist verantwortlich für die LDL-Rezeptorbindung. Die C-Apolipoproteine sind Oberflächenproteine der VLDL und werden bei deren Abbau auf die HDL übertragen; gleichzeitig haben sie spezifische Wirkungen auf die Lipoproteinlipase. Diese wird auch von den E-Apolipoproteinen beeinflußt, die sowohl in triglyceridreichen Lipoproteinen wie HDL vorkommen und für die Lipoproteinbindung an einen weiteren Zelloberflächenrezeptor verantwortlich sind. Ernährung und Medikamente, Hormone und Körpergewicht, Alkohol, Zigarettenrauchen und körperliches Training und schließlich Erkrankungen von Leber und Nieren beeinflussen Konzentration und Stoffwechsel der Apolipoproteine. Abschließend werden die Zusammenhänge mit der Arteriosklerose beim Menschen besprochen.
    Notes: Summary Twelve different apolipoproteins have been described in human serum. Apo A–I and apo A–II are essential for the structure of the HDL particles and for the function of LCAT activity. Apo B is the main protein in LDL but does also occur in the triglyceride-rich particles. Apo B represents the binding protein for the LDL-receptor pathway. The C-apolipoproteins are located on the surface of VLDL. They are transferred to HDL throughout the catabolism of VLDL and affect lipoprotein lipase activity. This enzyme is also affected by the E-apolipoproteins which occur in the triglyceride-rich particles as well as in HDL. Apo E is the binding site for another specific cell receptor. The concentration and metabolism of apolipoproteins is affected by diet, drugs, hormones, body weight, alcohol, cigarettes, physical exercises, liver and renal diseases. There is a close relation between apolipoproteins and atherosclerosis.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 39 (1982), S. 0 
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: Neurosecretory granules were obtained from neurolobes of porcine pituitary glands. From the granules, highly purified neurophysins were prepared by HPLC. According to polyacrylamide gel electrophoresis, isoelectric focusing, N- and C-terminal amino acid residue determination, and amino acid composition, the neurophysins I1 I2, and II were identical to the neurophysins obtained from whole posterior lobes. Since degradation could not have occurred, we conclude that neurophysin I1 and I2 originated in the neurosecretory granules.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 36 (1981), S. 0 
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: The crude neurophysin containing extract from posterior lobes of porcine pituitaries was roughly purified by gel chromatography. 15 mg of the lyophilized neurophysin complex were completely separated by HPLC yielding in neurophysin I1 (3.6 mg), I2 (4.0 mg), II (4.6 mg) and III (1.9 mg). All of the neurophysins were homogenous by PAGE and SDS-electrophoresis, isoelectrofocussing, amino-acid composition and N- and C-terminal amino acid analysis. In conclusion, HPLC is a reliable and quick method for the preparation of pure neurophysins.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Springer
    Fresenius' Zeitschrift für analytische Chemie 311 (1982), S. 430-431 
    ISSN: 1618-2650
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Conclusions The data demonstrate that even synthetic peptides have to be purified prior to testing biological activities and to immunization, because most commercially available peptides are impure. Furthermore, human insulin could be analyzed and characterized from tumor extracts using HPLC.
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    Springer
    Fresenius' Zeitschrift für analytische Chemie 301 (1980), S. 157-158 
    ISSN: 1618-2650
    Keywords: Best. von Apolipoprotein A I in Blutserum ; Immunoelektrophorese
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 7
    Electronic Resource
    Electronic Resource
    Springer
    Fresenius' Zeitschrift für analytische Chemie 317 (1984), S. 708-709 
    ISSN: 1618-2650
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 8
    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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