Skip to main content
PMC home page
Biochemical Journal logoLink to Biochemical Journal
. 1968 May;107(5):691–698. doi: 10.1042/bj1070691

Influence of temperature acclimatization on the ionic activation of goldfish intestinal adenosine triphosphatase

M W Smith 1, V E Colombo 1,*, E A Munn 1
PMCID: PMC1198722  PMID: 16742591

Abstract

1. An adenosine triphosphatase membrane system, dependent on Mg2+ and activated further by Na++K+, was prepared from goldfish anterior intestine by differential centrifugation of homogenized intestinal scrapings. 2. The affinity of this preparation for Na+ in the presence of K++Mg2+, for K+ in the presence of Na++Mg2+ and for Mg2+ alone, measured at 37°, did not depend on the previous environmental temperature of the fish. When Na++K+ were added to preparations from 8°-acclimatized fish the affinity for Mg2+ increased; this was not seen with preparations from 30°-acclimatized fish. 3. Part of the Mg2+-activated adenosine triphosphatase was inhibited by Na+ and the amount of inhibition appeared to increase at high acclimatization temperatures. 4. This Na+-inhibited adenosine triphosphatase was separated from the (Na++K+)-activated enzyme by centrifugation on sucrose density gradients. 5. Preparations from 8°-acclimatized fish contained less Mg2+-activated and more (Na++K+)-activated adenosine triphosphatase than did similar fractions from 30°-acclimatized fish. 6. Acclimatization to different environmental temperatures might involve one form of adenosine triphosphatase changing to another. The origin of various membranes seen in microsomal fractions must, however, be established before this hypothesis can be tested further.

Full text

PDF
698

Selected References

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

  1. Berg G. G., Chapman B. The sodium and potassium activated ATPase of intestinal epithelium. I. Location of enzymatic activity in the cell. J Cell Physiol. 1965 Jun;65(3):361–372. doi: 10.1002/jcp.1030650309. [DOI] [PubMed] [Google Scholar]
  2. Berg G. G., Szekerczes J. The sodium and potassium activated ATPase. II. Comparative study of intestinal epithelium and red cells. J Cell Physiol. 1966 Jun;67(3):487–500. doi: 10.1002/jcp.1040670313. [DOI] [PubMed] [Google Scholar]
  3. Epstein F. H., Katz A. I., Pickford G. E. Sodium- and potassium-activated adenosine triphosphatase of gills: role in adaptation of teleosts to salt water. Science. 1967 Jun 2;156(3779):1245–1247. doi: 10.1126/science.156.3779.1245. [DOI] [PubMed] [Google Scholar]
  4. FERNANDEZ-MORAN H. Cell-membrane ultrastructure. Low-temperature electron microsopy and x-ray diffraction studies of lipoprotein components in lamellar systems. Circulation. 1962 Nov;26:1039–1065. doi: 10.1161/01.cir.26.5.1039. [DOI] [PubMed] [Google Scholar]
  5. 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]
  6. SKOU J. C. ENZYMATIC BASIS FOR ACTIVE TRANSPORT OF NA+ AND K+ ACROSS CELL MEMBRANE. Physiol Rev. 1965 Jul;45:596–617. doi: 10.1152/physrev.1965.45.3.596. [DOI] [PubMed] [Google Scholar]
  7. SKOU J. C. Preparation from mammallian brain and kidney of the enzyme system involved in active transport of Na ions and K ions. Biochim Biophys Acta. 1962 Apr 9;58:314–325. doi: 10.1016/0006-3002(62)91015-6. [DOI] [PubMed] [Google Scholar]
  8. Smith M. W. Influence of temperature acclimatization on the temperature-dependence and ouabain-sensitizing of goldfish intestinal adenosine triphosphatase. Biochem J. 1967 Oct;105(1):65–71. doi: 10.1042/bj1050065. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. TAYLOR C. B. Cation-stimulation of an ATPase system from the intestinal mucosa of the guinea-pig. Biochim Biophys Acta. 1962 Jul 2;60:437–440. doi: 10.1016/0006-3002(62)90429-8. [DOI] [PubMed] [Google Scholar]
  10. ULRICH F. THE INHIBITION OF MITOCHONDRIAL ADENOSINE TRIPHOSPHATASE. THE EFFECTS OF ALKALI-METAL IONS. Biochem J. 1963 Aug;88:193–206. doi: 10.1042/bj0880193. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Biochemical Journal are provided here courtesy of The Biochemical Society

RESOURCES