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. 1967 Jan;102(1):294–303. doi: 10.1042/bj1020294

A study of the sulphur amino acids of rat tissues

Gerald E Gaull 1,*, M K Gaitonde 1
PMCID: PMC1270240  PMID: 6030290

Abstract

1. In a study of the metabolism of l-[35S]methionine in vivo, the labelled sulphur compounds of rat liver and brain were separated first by ion-exchange chromatography into two fractions containing (i) free sulphur amino acids such as methionine, cystathionine, cyst(e)ine and homocyst(e)ine and (ii) glutathione. 2. Two-dimensional paper chromatography with butan-1-ol–acetic acid or propionic acid–water in the first direction and 80% acetone or acetone–ethyl methyl ketone–water in the second direction was found superior to other solvent systems for separating the sulphur amino acids. 3. At 10min. after injection of [35S]methionine only a small part of the 35S was found combined in free methionine or other free sulphur amino acids. 4. Evidence was obtained of the presence of adenosyl[35S]methionine and adenosyl[35S]homocysteine in perchloric acid extracts of rat liver and brain. 5. The trans-sulphuration pathway was active in brain as well as in liver.

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Selected References

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  1. Alexander P., Hudson R. F., Fox M. The reaction of oxidizing agents with wool. 1. The division of cystine into two fractions of widely differing reactivities. Biochem J. 1950 Jan;46(1):27–32. doi: 10.1042/bj0460027. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. CARSON N. A., DENT C. E., FIELD C. M., GAULL G. E. HOMOCYSTINURIA: CLINICAL AND PATHOLOGICAL REVIEW OF TEN CASES. J Pediatr. 1965 Mar;66:565–583. doi: 10.1016/s0022-3476(65)80121-4. [DOI] [PubMed] [Google Scholar]
  3. CLAMP J. R., HOUGH L. THE PERIODATE OXIDATION OF AMINO ACIDS WITH REFERENCE TO STUDIES ON GLYCOPROTEINS. Biochem J. 1965 Jan;94:17–24. doi: 10.1042/bj0940017. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Dent C. E. A study of the behaviour of some sixty amino-acids and other ninhydrin-reacting substances on phenol-;collidine' filter-paper chromatograms, with notes as to the occurrence of some of them in biological fluids. Biochem J. 1948;43(2):169–180. [PMC free article] [PubMed] [Google Scholar]
  5. Dunstone J. R., Morgan W. T. Further observations on the glycoproteins in human ovarian cyst fluids. Biochim Biophys Acta. 1965 Nov 1;101(3):300–314. doi: 10.1016/0926-6534(65)90009-6. [DOI] [PubMed] [Google Scholar]
  6. GAITONDE M. K., DAHL D. R., ELLIOTT K. A. ENTRY OF GLUCOSE CARBON INTO AMINO ACIDS OF RAT BRAIN AND LIVER IN VIVO AFTER INJECTION OF UNIFORMLY 14-C-LABELLED GLUCOSE. Biochem J. 1965 Feb;94:345–352. doi: 10.1042/bj0940345. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. GAITONDE M. K., GORDON M. W. A microchemical method for the detection and determination of shikimic acid. J Biol Chem. 1958 Feb;230(2):1043–1050. [PubMed] [Google Scholar]
  8. GAITONDE M. K. RATE OF UTILIZATION OF GLUCOSE AND 'COMPARTMENTATION' OF ALPHA-OXOGLUTARATE AND GLUTAMATE IN RAT BRAIN. Biochem J. 1965 Jun;95:803–810. doi: 10.1042/bj0950803. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. GAITONDE M. K., RICHTER D. The metabolic activity of the proteins of the brain. Proc R Soc Lond B Biol Sci. 1956 Mar 27;144(918):83–99. doi: 10.1098/rspb.1956.0019. [DOI] [PubMed] [Google Scholar]
  10. GAITONDE M. K., RICHTER D. The uptake of 35S into tissues after injection of (35S) methionine. Biochem J. 1955 Apr;59(4):690–696. doi: 10.1042/bj0590690. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. GAITONDE M. K. The composition of brain lipoprotein fractions obtained by different procedures. J Neurochem. 1961 Dec;8:234–242. doi: 10.1111/j.1471-4159.1961.tb13548.x. [DOI] [PubMed] [Google Scholar]
  12. Gaitonde M. K. The rate of incorporation of [S]methionine and [S]cystine into proteolipids and proteins of rat brain. Biochem J. 1961 Aug;80(2):277–284. doi: 10.1042/bj0800277. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Gaull G., Gaitonde M. K. Homocystinuria: an observation on the inheritance of cystathionine synthase deficiency. J Med Genet. 1966 Sep;3(3):194–197. doi: 10.1136/jmg.3.3.194. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. KIRBY K. S. Some new solvent systems for the paper chromatography of nucleic acid degradation products. Biochim Biophys Acta. 1955 Dec;18(4):575–576. doi: 10.1016/0006-3002(55)90157-8. [DOI] [PubMed] [Google Scholar]
  15. MUDD S. H., FINKELSTEIN J. D., IRREVERRE F., LASTER L. HOMOCYSTINURIA: AN ENZYMATIC DEFECT. Science. 1964 Mar 27;143(3613):1443–1445. doi: 10.1126/science.143.3613.1443. [DOI] [PubMed] [Google Scholar]
  16. PALLADIN A. V., POLIAKOVA N. M., SILICH T. P. Sravnitel'noe izuchenie belkov mozga i nerva. Fiziol Zh SSSR Im I M Sechenova. 1957 Jul;43(7):611–618. [PubMed] [Google Scholar]
  17. PARKS L. W., SCHLENK F. The stability and hydrolysis of S-adenosylmethionine; isolation of S-ribosylmethionine. J Biol Chem. 1958 Jan;230(1):295–305. [PubMed] [Google Scholar]
  18. SCHLENK F., DEPALMA R. E. The formation of S-adenosylmethionine in yeast. J Biol Chem. 1957 Dec;229(2):1037–1050. [PubMed] [Google Scholar]
  19. SCHRAM E., MOORE S., BIGWOOD E. J. Chromatographic determination of cystine as cysteic acid. Biochem J. 1954 May;57(1):33–37. doi: 10.1042/bj0570033. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. SMITH R. L., SCHLENK F. Determination of adenine thiomethylriboside and 5-thiomethylribose, and their differentiation from methionine. Arch Biochem Biophys. 1952 Jul;38:159–165. doi: 10.1016/0003-9861(52)90019-2. [DOI] [PubMed] [Google Scholar]
  21. STEVENS A., SAKAMI W. Biosynthesis of methionine in liver. J Biol Chem. 1959 Aug;234(8):2063–2072. [PubMed] [Google Scholar]
  22. Sanger F. Fractionation of oxidized insulin. Biochem J. 1949;44(1):126–128. doi: 10.1042/bj0440126. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. TALLAN H. H., MOORE S., STEIN W. H. L-cystathionine in human brain. J Biol Chem. 1958 Feb;230(2):707–716. [PubMed] [Google Scholar]
  24. VRBA R., GAITONDE M. K., RICHTER D. The conversion of glucose carbon into protein in the brain and other organs of the rat. J Neurochem. 1962 Sep-Oct;9:465–475. doi: 10.1111/j.1471-4159.1962.tb04199.x. [DOI] [PubMed] [Google Scholar]
  25. WYATT G. R. The purine and pyrimidine composition of deoxypentose nucleic acids. Biochem J. 1951 May;48(5):584–590. doi: 10.1042/bj0480584. [DOI] [PMC free article] [PubMed] [Google Scholar]

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