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[Distribution of Some Hydrolases in the Rat Kidney (author's Transl)]

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Journal Histochemistry
Specialty Biochemistry
Date 1981 Jan 1
PMID 6266981
Citations 2
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Abstract

Most of the available histochemical methods and techniques (azodye, metal salt and indigogenic methods, cryostat, free-floating and lyophilized section techniques) and different modifications of these methods (different substrate concentrations, pH, temperature, incubation time e.g.) were applied to study the distribution of acid phosphatase (AcPB = after Barka and Anderson; AcPG = after Gomori), beta-glucuronidase (beta-Glu), aryl sulfatase (AS), beta-N-acetylglucosaminidase (NAG), acid 5'-nucleotidase (a5-Nucl), non-specific esterase (NE) and alkaline phosphatase (AlP) in the kidneys of rats of both sexes. The optimal conditions for the demonstration of these enzymes were established. As most important proved: the incubation of free-floating sections cut from "standard"-fixed (2 h in formol-calcium continued for another 18-22 h in the same fixative plus 0.88 M sucrose at 4 degrees C) kidney slices - only for AcPB and NE material fixed after Holt had to be used; the incubation for AlP and NE at 4 degrees C; final pH of the incubation medium for AcPB 5.5, AcPG 5.0 and NE 6.5; the use of Fast Garnet GBC Salt as coupler in the NE azo-dye reaction. Sex differences and for the female rats an increased activity during oestrus were established for all hydrolases studied. In particular the following results were obtained: AcPB, a5-Nucl and A1P are more intensive in male and AcPG in female S1 segments of the juxtamedullary nephrons in relation to the nephrons of the other parts of the cortex. In the medullary rays the NE and the a5-Nucl show a higher activity in the S2 segments of female rats demonstrate a more intensive activity for NAG and NE. This is true for AcPG and A1P in male rats. In the inner medulla a stronger beta-Glu activity in male rats and a stronger NAG activity in female rats is observed. The AcPB activity of the cortical distal tubules is higher in male rats.

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References
1.
Hopsu-Havu V, ARSTILA A, Helminen H, Kalimo H . Improvements in the method for the electron microscopic localization of arylsulphatase activity. Histochemie. 1967; 8(1):54-64. DOI: 10.1007/BF00279874. View

2.
Bell M, Barrnett R . The use of thiol-substituted carboxylic acids as histochemical substrates. J Histochem Cytochem. 1965; 13(8):611-28. DOI: 10.1177/13.8.611. View

3.
Hayashi M . Comparative histochemical localization of lysosomal enzymes in rat tissues. J Histochem Cytochem. 1967; 15(2):83-92. DOI: 10.1177/15.2.83. View

4.
Gomori G . Further studies on the histochemical specificity of phosphatases. Proc Soc Exp Biol Med. 1949; 72(2):449, illust. DOI: 10.3181/00379727-72-17464. View

5.
Jacobson N, Jorgensen F, Thomsen A . On the localization of some phosphatases in three different segments of the proximal tubules in the rat kidney. J Histochem Cytochem. 1967; 15(8):456-69. DOI: 10.1177/15.8.456. View