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. 1966 Apr;99(1):12–21. doi: 10.1042/bj0990012

The components of an α-glycerophosphate cycle and their relation to oxidative metabolism in the lens

M H Griffiths 1,*
PMCID: PMC1264950  PMID: 4290550

Abstract

1. The concentration of ATP in a lens brei is maintained when the brei is incubated in oxygen with α-glycerophosphate. Lack of α-glycerophosphate or incubation in nitrogen causes the concentration to decrease. α-Glycerophosphate has some effect under anaerobic conditions but this is not sufficient to account for the maintenance in oxygen. 2. Manometric experiments show that α-glycerophosphate enhances the respiration of lens preparations. This respiration can be further increased by the addition of ADP and is abolished by cyanide and antimycin. The inference from these experiments is that a mitochondrial system able to oxidize α-glycerophosphate is present, i.e. the particulate half of the α-glycerophosphate cycle. 3. More than the calculated proportion of NADH is used when limiting amounts of dihydroxyacetone phosphate are added to lens tissue in spectrophotometric experiments. Dihydroxyacetone phosphate is therefore regenerated and an α-glycerophosphate cycle is operative. 4. A preparation of a particulate α-glycerophosphate dehydrogenase that takes up oxygen with methylene blue as electron acceptor is described. 5. Methods for obtaining mitochondria from lens are compared, and a useful extraction medium is defined. 6. Mitochondria with activities of the same order of magnitude as those obtained from liver, with α-glycerophosphate and glutamate as substrates, are prepared from epithelium detached from the capsule; some respiratory control is observed.

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Selected References

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

  1. BERKOW J. W., PATZ A. DEVELOPMENTAL HISTOCHEMISTRY OF THE RAT EYE. Invest Ophthalmol. 1964 Feb;3:22–33. [PubMed] [Google Scholar]
  2. BORST P. The aerobic oxidation of reduced diphosphopyridine nucleotide formed by glycolysis in Ehrlich ascites-tumour cells. Biochim Biophys Acta. 1962 Feb 26;57:270–282. doi: 10.1016/0006-3002(62)91120-4. [DOI] [PubMed] [Google Scholar]
  3. BOXER G. E., SHONK C. E. Mitochondrial triose phosphate isomerase. Biochim Biophys Acta. 1960 Jan 1;37:194–196. doi: 10.1016/0006-3002(60)90114-1. [DOI] [PubMed] [Google Scholar]
  4. CHANCE B., WILLIAMS G. R. A simple and rapid assay of oxidative phosphorylation. Nature. 1955 Jun 25;175(4469):1120–1121. doi: 10.1038/1751120a0. [DOI] [PubMed] [Google Scholar]
  5. ESTABROOK R. W., SACKTOR B. alpha-Glycerophosphate oxidase of flight muscle mitochondria. J Biol Chem. 1958 Oct;233(4):1014–1019. [PubMed] [Google Scholar]
  6. FLETCHER K., MYANT N. B., TYLER D. D. The influence of thyroid hormone upon the metabolism of adenosine triphosphate in rat liver. J Physiol. 1962 Jul;162:345–357. doi: 10.1113/jphysiol.1962.sp006937. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Green D. E. alpha-Glycerophosphate dehydrogenase. Biochem J. 1936 Apr;30(4):629–644. doi: 10.1042/bj0300629. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. HESS R., PEARSE A. G. Histochemical and homogenization studies of mitochondrial alpha-glycerophosphate dehydrogenase in the nervous system. Nature. 1961 Aug 12;191:718–719. doi: 10.1038/191718a0. [DOI] [PubMed] [Google Scholar]
  9. HOCKWIN O. [Study of phosphate metabolism of the crystalline lens with the aid of ion exchange chromatography]. Albrecht Von Graefes Arch Ophthalmol. 1960;162:339–345. doi: 10.1007/BF00681921. [DOI] [PubMed] [Google Scholar]
  10. KIELLEY W. W., BRONK J. R. Oxidative phosphorylation in mitochondrial fragments obtained by sonic vibration. J Biol Chem. 1958 Jan;230(1):521–533. [PubMed] [Google Scholar]
  11. KINOSHITA J. H. Carbohydrate metabolism of lens. AMA Arch Ophthalmol. 1955 Sep;54(3):360–368. doi: 10.1001/archopht.1955.00930020366005. [DOI] [PubMed] [Google Scholar]
  12. KINOSHITA J. H., KERN H. L., MEROLA L. O. Factors affecting the cation transport of calf lens. Biochim Biophys Acta. 1961 Mar 4;47:458–466. doi: 10.1016/0006-3002(61)90541-8. [DOI] [PubMed] [Google Scholar]
  13. LEHNINGER A. L. Phosphorylation coupled to oxidation of dihydrodiphosphopyridine nucleotide. J Biol Chem. 1951 May;190(1):345–359. [PubMed] [Google Scholar]
  14. MYERS D. K., SLATER E. C. The enzymic hydrolysis of adenosine triphosphate by liver mitochondria. I. Activities at different pH values. Biochem J. 1957 Dec;67(4):558–572. doi: 10.1042/bj0670558. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. PENNINGTON R. J. Biochemistry of dystrophic muscle. Mitochondrial succinate-tetrazolium reductase and adenosine triphosphatase. Biochem J. 1961 Sep;80:649–654. doi: 10.1042/bj0800649. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. PIRIE A. Metabolism of glycerophosphate in the lens. Exp Eye Res. 1962 Jun;1:427–435. doi: 10.1016/s0014-4835(62)80034-7. [DOI] [PubMed] [Google Scholar]
  17. PURVIS J. L., LOWENSTEIN J. M. The relation between intra- and extramitochondrial pyridine nucleotides. J Biol Chem. 1961 Oct;236:2794–2803. [PubMed] [Google Scholar]
  18. RINGLER R. L., SINGER T. P. Solubilization and assay of the insoluble alpha-glycero-phosphate dehydrogenase of animal tissues. Biochim Biophys Acta. 1958 Sep;29(3):661–662. doi: 10.1016/0006-3002(58)90036-2. [DOI] [PubMed] [Google Scholar]
  19. RINGLER R. L., SINGER T. P. Studies on the mitochondrial alpha-glycerophosphate dehydrogenase. I. Reaction of the dehydrogenase with electron acceptors and the respiratory chain. J Biol Chem. 1959 Aug;234(8):2211–2217. [PubMed] [Google Scholar]
  20. SACKTOR B., COCHRAN D. G. The respiratory metabolism of insect flight muscle. I. Manometric studies of oxidation and concomitant phosphorylation with sarcosomes. Arch Biochem Biophys. 1958 Mar;74(1):266–276. doi: 10.1016/0003-9861(58)90219-4. [DOI] [PubMed] [Google Scholar]
  21. SACKTOR B., DICK A. Pathways of hydrogen transport in the oxidation of extramitochondrial reduced diphosphopyridine nucleotide in flight muscle. J Biol Chem. 1962 Oct;237:3259–3263. [PubMed] [Google Scholar]
  22. SIPPEL T. O. Measurement of oxygen consumption in the rat lens with a flow respirometer. Invest Ophthalmol. 1962 Jun;1:377–384. [PubMed] [Google Scholar]
  23. VAN HEYNINGEN R. Metabolism of xylose by the lens; calf lens in vitro. Biochem J. 1958 Aug;69(4):481–491. doi: 10.1042/bj0690481a. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. VIRMAUX N., MANIEL P. Succinic dehydrogenase activity and oxidative phosphorylation of the mitochondria in the crystalline lens of bovines. Nature. 1963 Feb 23;197:792–793. doi: 10.1038/197792a0. [DOI] [PubMed] [Google Scholar]
  25. WANKO T., GAVIN M. A. Electron microscope study of lens fibers. J Biophys Biochem Cytol. 1959 Aug;6(1):97–102. doi: 10.1083/jcb.6.1.97. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. WANKO T., GAVIN M. A. The fine structure of the lens epithelium; an electron microscopic study. AMA Arch Ophthalmol. 1958 Nov;60(5):868–879. doi: 10.1001/archopht.1958.00940080888007. [DOI] [PubMed] [Google Scholar]
  27. WEINBACH E. C. A procedure for isolating stable mitochondria from rat liver and kidney. Anal Biochem. 1961 Aug;2:335–343. doi: 10.1016/0003-2697(61)90006-9. [DOI] [PubMed] [Google Scholar]
  28. WEINBACH E. C., SHEFFIELD H., GARBUS J. RESTORATION OF OXIDATIVE PHOSPHORYLATION AND MORPHOLOGICAL INTEGRITY TO SWOLLEN, UNCOUPLED RAT LIVER MITOCHONDRIA. Proc Natl Acad Sci U S A. 1963 Sep;50:561–568. doi: 10.1073/pnas.50.3.561. [DOI] [PMC free article] [PubMed] [Google Scholar]
  29. WEINBACH E. C. Stability of oxidative phosphorylation and related reactions in isolated liver mitochondria. J Biol Chem. 1959 Jun;234(6):1580–1586. [PubMed] [Google Scholar]
  30. van den BERGH S., SLATER E. C. The respiratory activity and permeability of housefly sarcosomes. Biochem J. 1962 Feb;82:362–371. doi: 10.1042/bj0820362. [DOI] [PMC free article] [PubMed] [Google Scholar]

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