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  • Articles: DFG German National Licenses  (2)
  • 2005-2009
  • 1970-1974  (2)
  • 1965-1969
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  • Pancreas
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  • Articles: DFG German National Licenses  (2)
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  • 2005-2009
  • 1970-1974  (2)
  • 1965-1969
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  • 1
    ISSN: 1432-2013
    Keywords: Pancreas ; Acini ; Ducts ; Membrane Enzymes
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Enzymes activities of the Na+K+-and the HCO3 −-ATPases, alkaline phosphatase, amino peptidase and 5′ nucleotidase have been measured in 4 different preparations from the cat pancreas a) in the ducts including all sizes b) in ducts of three different diameters c) in that tissue, which had been dissected off from the ducts, called “acini”, and d) in the whole homogenate of the pancreas. The distribution of the measured enzymes shows, that the Na+K+-activity is highest in the acinar structures (mean value 0.532 μM/mg Protein x h), while the ducts show nearly no Na+K+-ATPase activity. The HCO3 −-ATPase, the alkaline phosphatase and the 5′ nucleotidase are in the ducts between 2.4 and 3.6 times higher than in the whole organ whereas the amino peptidase does not appear to have a selective distribution. As the HCO3 −-ATPase activity distribution pattern is identical with that of the secretory capacity of HCO3 − as evidenced by earlier micropuncture studies, the data suggest that the HCO3 −-ATPase is the main enzyme involved in the secretion of the bicarbonate buffer. Concerning the Na+K+-ATPase activity in the acinar structures we cannot contribute to its function in the enzyme secreting process.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Acta diabetologica 9 (1972), S. 350-357 
    ISSN: 1432-5233
    Keywords: Insulin biosynthesis ; Insulin metabolism ; Liver ; Pancreas
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Description / Table of Contents: Resumen Les modes de transformation de l'insuline dans le foie ont été étudiés par nombre d'acides aminés marqués avec14C injectés en même temps. L'insuline, isolée du pancréas et du fois et contenant des résidus de14C-glycine,14C-sérine et14C-alanine a été séparée dans les chaînes A et B; celles-ci ont été ensuite soumises à l'hydrolyse acide complète, suivie par la détermination de l'activité spécifique de chaque résidu acide aminé. Les rapports entre les activités des résidus glycine et alanine de l'insuline isolée du foie diffèrent considérablement de ceux de l'insuline isolée du pancréas; la différence et moins sensible en ce qui concerne les résidus de la sérine et elle est presque totalement absente quant aux résidus de la thyroxine. Il existe des raisons valables de croire que dans le tissu hépatique la nouvelle synthèse de l'insuline se vérifie partant des résidus les plus petits des chaînes A et B.
    Abstract: Résumé Las modalidades de transformación de la insulina en el hígado han sido estudiadas utilizando numerosos aminoácidos marcados con14C, inyectados simultáneamente. En las cadenas A y B se ha escindido la insulina con presencia de residuos de14C-glicina,14C-serina y14C-alanina aislada del páncreas y del hígado; ambas cadenas han sido sometidas después a hidrolisis ácida completa, determinando a continuación la actividad específica de cada residuo aminoácido. Las relaciones entre las actividades específicas de los residuos glicina y alanina de la insulian aislada del hígado, difieren notablemente de los de la insulina aislada del páncreas; la diferencia es menor por lo que se refiere a los residuos de serina y casi inexistente en lo referente a los de tiroxina. Tenemos, pues, razones suficientes para suponer que en el tejido hepático la resistencia a la insulina tenga lugar a partir de los residuos más pequeños de las cadenas A y B.
    Notes: Riassunto Le modalità di trasformazione dell'insulina nel fegato sono state studiate mediante l'impiego di numerosi aminoacidi marcati con14C, iniettati contemporaneamente. L'insulina isolata dal pancreas e dal fegato e contenente residui di14C-glicina,14C-serina e14C-alanina è stata scissa nelle catene A e B; queste sono state poi sottoposte ad idrolisi acida completa, seguita da determinazione dell'attività specifica di ciascun residuo aminoacidico. I rapporti tra le attività specifiche dei residui della glicina e della alanina dell'insulina isolata dal fegato differiscono notevolmente da quelli dell'insulina isolata dal pancreas; la differenza è meno marcata per quanto riguarda i residui della serina e quasi del tutto assente per quelli della tirosina. Esistono validi motivi per pensare che nel tessuto epatico la resintesi dell'insulina abbia luogo a partire da residui più piccoli delle catene A e B.
    Type of Medium: Electronic Resource
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