Skip to main content
PMC home page
Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1969 Jun;63(2):412–419. doi: 10.1073/pnas.63.2.412

COMPARISON OF RAT LIVER MITOCHONDRIAL AND MICROSOMAL MEMBRANE PROTEINS

Carl A Schnaitman 1
PMCID: PMC223580  PMID: 5257131

Abstract

An improved method is described for dissolving membrane proteins and for resolving them by polyacrylamide gel electrophoresis. With this procedure, the inner mitochondrial membrane has been found to contain 23 different protein species and the outer membrane 12. Only one protein species appears to be common to the two membranes. Smooth and rough microsomal membranes contain 15 different proteins. The approximate molecular weight and relative amount of each protein species have been extrapolated from the gel patterns. The outer mitochondrial membrane and the smooth microsomal membrane contain at least three protein species that appear to be identical, suggesting that they possess a common origin.

Full text

PDF
412

Selected References

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

  1. Beattie D. S., Basford R. E., Koritz S. B. The inner membrane as the site of the in vitro incorporation of L-[14C]leucine into mitochondrial protein. Biochemistry. 1967 Oct;6(10):3099–3106. doi: 10.1021/bi00862a017. [DOI] [PubMed] [Google Scholar]
  2. CLARKE J. T. SIMPLIFIED "DISC" (POLYACRYLAMIDE GEL) ELECTROPHORESIS. Ann N Y Acad Sci. 1964 Dec 28;121:428–436. doi: 10.1111/j.1749-6632.1964.tb14214.x. [DOI] [PubMed] [Google Scholar]
  3. Dallner G., Bergstrand A., Nilsson R. Heterogeneity of rough-surfaced liver microsomal membranes of adult, phenobarbital-treated, and newborn rats. J Cell Biol. 1968 Aug;38(2):257–276. doi: 10.1083/jcb.38.2.257. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. FOLCH J., ASCOLI I., LEES M., MEATH J. A., LeBARON N. Preparation of lipide extracts from brain tissue. J Biol Chem. 1951 Aug;191(2):833–841. [PubMed] [Google Scholar]
  5. Farmbrough D. M., Fujimura F., Bonner J. Quantitative distribution of histone components in the pea plant. Biochemistry. 1968 Feb;7(2):575–585. doi: 10.1021/bi00842a010. [DOI] [PubMed] [Google Scholar]
  6. GREEN D. E., TISDALE H. D., CRIDDLE R. S., CHEN P. Y., BOCK R. M. Isolation and properties of the structural protein of mitochondria. Biochem Biophys Res Commun. 1961 Jun 2;5:109–114. doi: 10.1016/0006-291x(61)90021-3. [DOI] [PubMed] [Google Scholar]
  7. Green D. E., Haard N. F., Lenaz G., Silman H. I. On the noncatalytic proteins of membrane systems. Proc Natl Acad Sci U S A. 1968 May;60(1):277–284. doi: 10.1073/pnas.60.1.277. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Haldar D., Freeman K., Work T. S. Biogenesis ommitochondria. Nature. 1966 Jul 2;211(5044):9–12. doi: 10.1038/211009a0. [DOI] [PubMed] [Google Scholar]
  9. Maizel J. V., Jr Acrylamide-gel electrophorograms by mechanical fractionation: radioactive adenovirus proteins. Science. 1966 Feb 25;151(3713):988–990. doi: 10.1126/science.151.3713.988. [DOI] [PubMed] [Google Scholar]
  10. Okamoto H., Yamamoto S., Nozaki M., Hayaishi O. On the submitochondrial localization of l-kynurenine-3-hydroxylase. Biochem Biophys Res Commun. 1967 Feb 8;26(3):309–314. doi: 10.1016/0006-291x(67)90123-4. [DOI] [PubMed] [Google Scholar]
  11. Orrenius S., Ericsson J. L., Ernster L. Phenobarbital-induced synthesis of the microsomal drug-metabolizing enzyme system and its relationship to the proliferation of endoplasmic membranes. A morphological and biochemical study. J Cell Biol. 1965 Jun;25(3):627–639. doi: 10.1083/jcb.25.3.627. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. RICHARDSON S. H., HULTIN H. O., GREEN D. E. STRUCTURAL PROTEINS OF MEMBRANE SYSTEMS. Proc Natl Acad Sci U S A. 1963 Nov;50:821–827. doi: 10.1073/pnas.50.5.821. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Schnaitman C., Greenawalt J. W. Enzymatic properties of the inner and outer membranes of rat liver mitochondria. J Cell Biol. 1968 Jul;38(1):158–175. doi: 10.1083/jcb.38.1.158. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Shapiro A. L., Viñuela E., Maizel J. V., Jr Molecular weight estimation of polypeptide chains by electrophoresis in SDS-polyacrylamide gels. Biochem Biophys Res Commun. 1967 Sep 7;28(5):815–820. doi: 10.1016/0006-291x(67)90391-9. [DOI] [PubMed] [Google Scholar]
  15. Silman H. I., Rieske J. S., Lipton S. H., Baum H. A new protein component of complex 3 of the mitochondrial electron transfer chain. J Biol Chem. 1967 Nov 10;242(21):4867–4875. [PubMed] [Google Scholar]
  16. Sottocasa G. L., Kuylenstierna B., Ernster L., Bergstrand A. An electron-transport system associated with the outer membrane of liver mitochondria. A biochemical and morphological study. J Cell Biol. 1967 Feb;32(2):415–438. doi: 10.1083/jcb.32.2.415. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Takayama K., MacLennan D. H., Tzagoloff A., Stoner C. D. Studies on the electron transfer system. LXVII. Polyacrylamide gel electrophoresis of the mitochondrial electron transfer complexes. Arch Biochem Biophys. 1966 Apr;114(1):223–230. doi: 10.1016/0003-9861(66)90324-9. [DOI] [PubMed] [Google Scholar]
  18. Zahler P. H., Wallach D. F. Isolation of lipid-free plasma membrane proteins by gel filtration on Sephadex LH-20 using 2-chloroethanol-water as solvent. Biochim Biophys Acta. 1967 May 2;135(2):371–374. doi: 10.1016/0005-2736(67)90135-6. [DOI] [PubMed] [Google Scholar]
  19. Zahler P. Blood group antigens in relation to chemical and structural properties of the red cell membrane. Vox Sang. 1968;15(2):81–101. doi: 10.1111/j.1423-0410.1968.tb03414.x. [DOI] [PubMed] [Google Scholar]

Articles from Proceedings of the National Academy of Sciences of the United States of America are provided here courtesy of National Academy of Sciences

RESOURCES