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  • 1
    Electronic Resource
    Electronic Resource
    An Aminopeptidase Occurring in Pig Kidney. I. An Improved Method of Preparation. Physical and Enzymic Properties* (1966)
    s.l. : American Chemical Society
    Biochemistry 5 (1966), S. 169-174 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00865a022
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  • 2
    Electronic Resource
    Electronic Resource
    An Aminopeptidase Occurring in Pig Kidney. II. A Study on the Mechanism of the Hydrolysis* (1966)
    s.l. : American Chemical Society
    Biochemistry 5 (1966), S. 175-182 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00865a023
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    The cellular distribution of aldolase isozymes in rat kidney and brain determined in tissue sections by the immuno-histochemical method (1975)
    Springer
    Histochemistry and cell biology 45 (1975), S. 143-161 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The use of the immuno-histochemical method permits the localization of aldolase isozymes in tissue sections. Upon incubating a section with a monomer-specific antiserum, isozymes containing that monomer remain in the section, whereas other cytoplasmic enzymes diffuse out of the section. If soluble antigen is added subsequently, it is bound by the tissue-bound antibody. These antibody fixed aldolases can then be stained by the use of a tetrazolium test linked to substrate hydrolysis. In this way it was demonstrated that isozymes of aldolase containing mostly the A monomer are predominantly localized in the distal tubules, the collecting tubules, the vessels and capillaries of the kidney, the ganglia, the Purkinje cells, the neurons, the white matter and the chorioid plexus of the brain. Aldolase containing mostly B-monomers were found in the proximal tubules. Aldolase isozymes particularly rich in C-monomers were seen in the nervus opticus, the pia mater, the vessels of cerebrum and the molecular layer of the cortex cerebelli.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00495158
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  • 4
    Electronic Resource
    Electronic Resource
    Lokalisation von Aminopeptidase in Gewebeschnitten mit einer neuen Immunofluoreszenztechnik (1968)
    Springer
    Histochemistry and cell biology 14 (1968), S. 282-296 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Description / Table of Contents: Zusammenfassung Die Lokalisation von Aminopeptidase in verschiedenen Schweinegeweben wurde mit Hilfe einer immunochemischen Fluorezenzmethode durchgeführt. Als Reagentien zur Kopplung mit dem im Gewebe fixierten Enzym dienten Antigen-Antikörper-Präzipitate von partikelgebundener Aminopeptidase, rein dargestellt aus Schweinenieren, mit ihrem Kaninchen Antikörper. Der Bindungsort wurde mit fluoreszenz-markiertem Anti-Kaninchen-γ-Globulin bestimmt. Mit dieser Methode war Aminopeptidase in praktisch allen Geweben nachweisbar, doch variierte die Konzentration. Besonders reichhaltig an diesem Enzym sind Zellen mit bevorzugt sekretorischer und resorptiver Funktion. Aminopeptidase befindet sich im Bereich der Mikrovilli und der Pinozytosebläschen, aber auch in dem der lamellären Saftspalten des Bindegewebes. Enzymatische und immunochemische Vergleichsuntersuchungen bestätigen diese Befunde. Aminopeptidase ist demnach im Bereich von stoffwechselaktiven Grenzflächen lokalisiert und wahrscheinlich als Mukopolysaccharid-Komplex gebunden.
    Notes: Summary Aminopeptidase was localised in different pig tissues by an immunochemical fluorescense method. The reagent for coupling with the tissue fixed enzyme consisted of antigen-antibody-precipitates derived from purified particle bound pig kidney aminopeptidase with its rabbit antiserum. Any subsequent binding was demonstrated by staining with fluorescent labelled anti-rabbit-γ-globulin. By this method aminopeptidase was found in practically all tissues in varying concentrations, particullarly in cells having resorptive or secretory function. Aminopeptidase is present in the region of the microvilli and pinocytotic vesicles of cells and also in the amorphous groundsubstance of loose connective tissue. Comparative enzymatic and immunochemical studies have confirmed these results. Thus aminopeptidase is situated in boundary surfaces, which have high intermediary metabolic activity. It is probably bound as a mucopolysaccharide complex.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00306324
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  • 5
    Electronic Resource
    Electronic Resource
    The differentiation of proximal and distal tubules in the male rat kidney: The appearance of aldolase isozymes, aminopeptidase and alkaline phosphatase during ontogeny (1976)
    Springer
    Histochemistry and cell biology 47 (1976), S. 315-337 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary 1. The specific activities of aminopeptidase, alkaline phosphatase and aldolase isozymes were measured in homogenates of kidneys taken at different stages of ontogeny. The cellular localization of these enzymes was studied in cryostat tissue sections using substrate linked assays for aminopeptidase and alkaline phosphatase and the mixed aggregation immuno-cytochemical technique for aldolase isozymes; local enzyme concentrations were estimated photometrically. 2. The presence of both aldolase-A and aldolase-B was demonstrated in all metanephrogenic cells (and at still higher concentrations in collecting tubule cells) of the rat fetus 16 days after conception and in the undifferentiated cells of the neogenetic zone of kidney up to 8 days after birth; no aminopeptidase or alkaline phosphatase could be found in these cells. 3. Measurements made on stained tissue sections show that the shift towards aldolase-B, seen in homogenate analyses, is due to a change in the relative amounts of proximal tubules. No evidence was seen for repression in the synthesis of aldolase-A or aldolase-B monomers in the different kidney cells during ontogeny. 4. Two transitions in the mode of nephron differentiation were observed: one was shortly after birth, the other followed weaning. Before the first transition the concentrations of the enzymes increased to different degrees, such that the enzymes reached concentrations comparable with those as in the cells of adult rats by 2 to 4 days post partum. After the second transition proximal tubule size and specific activity of brush border membrane enzymes increased 3 fold. In contrast, the distal tubules did not increase significantly in size, but their aldolase-A concentration increased 3 fold. 5. Evidence based on enzyme quantification and morphometry in kidney sections is presented to demonstrate that the proximal tubule cells show functional adaptation by two independent mechanisms: specific amplification of gene expression and hypertrophy. In contrast, the distal tubule shows functional adaptation only by specific amplification of gene expression.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00489199
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  • 6
    Electronic Resource
    Electronic Resource
    Differentiation of epithelial cells in human jejunum: Localization and quantification of aminopeptidase, alkaline phosphatase and aldolase isozymes in tissue sections (1976)
    Springer
    Histochemistry and cell biology 48 (1976), S. 101-109 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Sections from human jejunum were stained histochemically for aminopeptidase and alkaline phosphatase and the aldolase isozymes were detected with the mixed aggregation immuno-cytochemical technique. All enzyme concentrations increased from the bottom to the upper part of the crypt. The concentration of aldolase-A per cell was the same in the upper part of the crypt and the villus, whereas the concentration of the other three enzymes was still higher. Therefore, high amounts of aldolase-B, aminopeptidase and alkaline phosphatase are present in cells highly active in absorption in a fashion similar to that found in the proximal tubule cells of kidney. The relatively undifferentiated cells of the crypts contained both aldolase-A and aldolase-B. Alkaline phosphatase gains its full activity later than aminopeptidase. The synthesis of microvillar membrane enzymes comes to an end earlier than that of the cytosol enzymes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00494548
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  • 7
    Electronic Resource
    Electronic Resource
    Conclusions about aminopeptidase in tissue sections from studies of amino acid naphthylamide hydrolysis (1976)
    Springer
    Histochemistry and cell biology 47 (1976), S. 271-283 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Catalytic properties (KM, Vmax) of aminopeptidase in pig kidney sections, in isolated membranes and in a solubilized purified form were investigated using amino acid 2-naphthylamides and 4-methoxy-2-naphthylamides. In the first case these properties were estimated on the basis of the stain intensity resulting from the coupling of product with Fast Blue B, in the latter two cases they were measured fluorometrically. The following observations were made: (1) In all three cases the substrate turnover was shown to be a direct function of time and enzyme concentration. (2) The values obtained for the solubilized and the membrane bound form were practically identical but differed from those found in tissue sections. (3) Each amino acid derivative had defined constants, but these were difficult to obtain in sections, especially if it was necessary, on account of poor solubilities, to use low substrate concentrations. (4) Hydrophilic amino acid derivatives were adsorbed to tissue membranes much less than hydrophobic ones. (5) Fast Blue B caused a non-competitive inhibition of enzymic activity. (6) Binding of antibody against pure aminopeptidase caused inhibition of the enzymic hydrolysis of all the naphthylamides. Thus, histochemical stain intensities per time and area derived from one substrate at a defined concentration are suitable for the determination of enzyme concentrations. However, no conclusions regarding the homogeneity of the enzyme in sections can be drawn by comparing the stain intensities obtained with different substrates in contrast to data from the inhibition of substrate hydrolysis by antibody.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00489195
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  • 8
    Electronic Resource
    Electronic Resource
    A comparison of the highly selective fluorescence staining of fungi in tissue sections with Uvitex 2B and Calcofluor White M2R (1988)
    Springer
    Journal of molecular histology 20 (1988), S. 215-221 
    Details
    ISSN: 1573-6865
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The selective fluorescence staining of two fungi,Candida albicans andBlastomyces dermatitides, with Uvitex 2B and Calcofluor White M2R was studied in deparaffinized and frozen sections of mouse kidney and lung. Both fluorochromes emitted maximally at about 430nm, independent of the mounting media (Kaiser's gelatin or Entellan). In addition to fungi, both fluorochromes also stained elastic fibres. The fluorescence intensity remained unchanged after storage of sections for more than 6 months in conventional slide boxes. the two fluorochromes showed the following differences: Calcofluor faded 1.25 times faster than Uvitex when illuminated with ultraviolet light. Calcofluor showed a greater affinity for tissues in general, and red cells and renal tubular casts in particular. Counterstaining of deparaffinized sections with Hemalum and Eosin reduced the fungi fluorescence and suppressed the general background fluorescence. However, it led to an intensification of Eosin staining and the fluorescence of red cells in Calcofluorstained sections but not in Uvitex-stained ones. Similarly, the background fluorescence in frozen sections was reduced by Evans Blue, although elastic fibres still fluoresced after staining with Calcofluor. The degree of staining selectivity, and thus the contrast produced within a histological specimen, was greater with Uvitex 2B than with Calcofluor White M2R.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01747466
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