Skip to main content
PMC home page
British Journal of Pharmacology logoLink to British Journal of Pharmacology
. 1970 May;39(1):87–98. doi: 10.1111/j.1476-5381.1970.tb09558.x

Localization of kininogenase in the rat kidney

K Nustad
PMCID: PMC1702930  PMID: 4315991

Abstract

1. The rat kidney kininogenase (KGA) activity was located mainly in the kidney cortex.

2. Differential centrifugation of kidney cortex homogenate revealed that the microsomal fraction contained more KGA activity per unit of protein than the other subcellular fractions.

3. Subfractionation of the microsomal fraction showed that the KGA activity was recovered in a subfraction also containing high specific activity of both alkaline phosphate and glucose-6-phosphatase. It is suggested that the KGA activity is localized in the plasma membrane and/or endoplasmic reticulum membranes of kidney cortical cells.

4. Hydrolysis of N-α-benzoyl-L-arginine ethyl ester at pH 8·5 paralleled the KGA activity.

Full text

PDF
87

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Abe K. Urinary excretion of kinin in man with special reference to its origin. Tohoku J Exp Med. 1965 Nov 25;87(2):175–184. doi: 10.1620/tjem.87.175. [DOI] [PubMed] [Google Scholar]
  2. BEAUFAY H., BENDALL D. S., BAUDHUIN P., DE DUVE C. Tissue fractionation studies. 12. Intracellular distribution of some dehydrogenases, alkaline deoxyribonuclease and iron in rat-liver tissue. Biochem J. 1959 Dec;73:623–628. doi: 10.1042/bj0730623. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. BONTING S. L., POLLAK V. E., MUEHRCKE R. C., KARK R. M. Quantitative histochemistry of the nephron. II. Alkaline phosphatase activity in man and other species. J Clin Invest. 1960 Sep;39:1372–1380. doi: 10.1172/JCI104156. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Baudhuin P., Beaufay H., Rahman-Li Y., Sellinger O. Z., Wattiaux R., Jacques P., De Duve C. Tissue fractionation studies. 17. Intracellular distribution of monoamine oxidase, aspartate aminotransferase, alanine aminotransferase, D-amino acid oxidase and catalase in rat-liver tissue. Biochem J. 1964 Jul;92(1):179–184. doi: 10.1042/bj0920179. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Carvalho I. F., Diniz C. R. Kinin-forming enzyme (kininogenin) in homogenates of rat kidney. Biochim Biophys Acta. 1966 Oct 17;128(1):136–148. doi: 10.1016/0926-6593(66)90150-0. [DOI] [PubMed] [Google Scholar]
  6. DE DUVE C., PRESSMAN B. C., GIANETTO R., WATTIAUX R., APPELMANS F. Tissue fractionation studies. 6. Intracellular distribution patterns of enzymes in rat-liver tissue. Biochem J. 1955 Aug;60(4):604–617. doi: 10.1042/bj0600604. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. DE DUVE C., WATTIAUX R. Tissue fractionation studies. VII. Release of bound hydrolases by means of triton X-100. Biochem J. 1956 Aug;63(4):606–608. doi: 10.1042/bj0630606. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Dallner G., Ernster L. Subfractionation and composition of microsomal membranes: a review. J Histochem Cytochem. 1968 Oct;16(10):611–632. doi: 10.1177/16.10.611. [DOI] [PubMed] [Google Scholar]
  9. De Duve C. Principles of tissue fractionation. J Theor Biol. 1964 Jan;6(1):33–59. doi: 10.1016/0022-5193(64)90065-7. [DOI] [PubMed] [Google Scholar]
  10. GOLDFISCHER S., ESSNER E., NOVIKOFF A. B. THE LOCALIZATION OF PHOSPHATASE ACTIVITIES AT THE LEVEL OF ULTRASTRUCTURE. J Histochem Cytochem. 1964 Feb;12:72–95. doi: 10.1177/12.2.72. [DOI] [PubMed] [Google Scholar]
  11. HERS H. G., BERTHET J., BERTHET L., DE DUVE C. Le système hexose-phosphatasique. III. Localisation intra-cellulaire des ferments par centrifugation fractionnée. Bull Soc Chim Biol (Paris) 1951;33(1-2):21–41. [PubMed] [Google Scholar]
  12. HUTCHISON W. C., MUNRO H. N. The determination of nucleic acids in biological materials. A review. Analyst. 1961 Dec;86:768–813. doi: 10.1039/an9618600768. [DOI] [PubMed] [Google Scholar]
  13. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  14. Mattenheimer H. Enzymology of kidney tissue. Curr Probl Clin Biochem. 1968;2:119–145. [PubMed] [Google Scholar]
  15. Nustad K. The relationship between kidney and urinary kininogenase. Br J Pharmacol. 1970 May;39(1):73–86. doi: 10.1111/j.1476-5381.1970.tb09557.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Rosen S., Coughlan M., Barry K. G. Renal acid phosphatase: a biochemical study. Lab Invest. 1966 Dec;15(12):1848–1855. [PubMed] [Google Scholar]
  17. WACHSTEIN M. Histochemical staining reactions of the normally functioning and abnormal kidney. J Histochem Cytochem. 1955 Jul;3(4):246–270. doi: 10.1177/3.4.246. [DOI] [PubMed] [Google Scholar]
  18. WERLE E., VOGEL R. [On the excretion of kallikrein in urine after experimental kidney injury]. Arch Int Pharmacodyn Ther. 1960 Jun 1;126:171–186. [PubMed] [Google Scholar]
  19. WERLE E., VOGEL R. [On the release of a kallikrein-like substance by extracts of various organs]. Arch Int Pharmacodyn Ther. 1961 May 1;131:257–261. [PubMed] [Google Scholar]
  20. Wattiaux-De Coninck S., Rutgeerts M. J., Wattiaux R. Lysosomes in rat-kidney tissue. Biochim Biophys Acta. 1965 Sep 20;105(3):446–459. doi: 10.1016/s0926-6593(65)80230-2. [DOI] [PubMed] [Google Scholar]
  21. Werle E., Leysath G., Schmal A. Uber das Verhalten des Kininogenspiegels nach Nieren- und nach Nebennierenexstirpation bei der Ratte. Hoppe Seylers Z Physiol Chem. 1968 Jan;349(1):107–108. [PubMed] [Google Scholar]

Articles from British Journal of Pharmacology are provided here courtesy of The British Pharmacological Society

RESOURCES