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  • Renal tubule  (2)
  • 1975-1979  (2)
  • 1935-1939
  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Pflügers Archiv 371 (1977), S. 141-145 
    ISSN: 1432-2013
    Keywords: Renal tubule ; Disaccharide reabsorption ; Maltase ; Brush border enzymes ; Microperfusion
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Renal tubular reabsorption of maltose, sucose and lactose were studied in vivo et situ by continuous microperfusion of single proximal convolutions of rat kidney. The14C-label of maltose (2.5 mmol/l) was removed from the lumen of the proximal tubule at about the same rate as found for glucose. Maltose reabsorption was completely inhibited in presence of 30 mmol/l glucose or of 0.1 mmol/l phlorizin. Chemical analysis of the samples showed a complete conversion of maltose into glucose within a perfusion distance of 2 mm. It is concluded from these results that within the tubular lumen maltose is split very rapidly by a brush border glucosidase. The short half time of this process permits the breakdown product glucose to be almost completely reabsorbed subsequently within the proximal tubule. In contrast, sucrose and lactose were neither split nor reabsorbed by the tubule brush border.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1432-2013
    Keywords: Amino acid transport ; Renal tubule ; Stereospecificity ; Passive diffusion ; Saturation kinetics
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Renal tubular reabsorption of glycine and of thel- andd-isomers of histidine, serine, phenylalamine, methionine, proline and cystine was investigated in vivo et situ by continuous microperfusion of single proximal convolutions of the rat kidney. In the case of glycine and thel-isomers, tubular reabsorption is saturable to a great extent. Thed-amino acids are reabsorbed much more slowly than the respectivel-forms. Furthermore in the case of methionine and perhaps also of proline, serine and phenylalanine, the fractional reabsorption decreases in the presence of high concentrations of thel-form. This indicates that thed-isomers also have a measurable affinity for the reabsorption mechanisms of the renal tubule. The very poor reabsorption ofd-amino acids in the presence of theirl-isomers indicates that simple passive diffusion plays only a relatively small role in tubular amino acid reabsorption. Permeability coefficients estimated from these findings are in the range from 1–5×10−7 cm2·s−1. These values are very similar to those found for other organic molecules of comparable molecular weights.
    Type of Medium: Electronic Resource
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