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Serum Sulfhydryl Determinations and Significance in Connective Tissue Diseases
76
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24
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1964
Year
PathologyChemical BiologyRedox BiologyOxidative StressInflammationGlobulin FractionationBioanalysisHuman Serum MacroglobulinsClinical ChemistryProteomicsLaboratory MedicineCell SignalingRheumatoid ArthritisMolecular SignalingRedox SignalingRheumatologyBiochemistryBiochemical InteractionChemical PathologyBiomolecular InteractionReactive Oxygen SpeciePharmacologyBiomolecular ScienceNatural SciencesCellular BiochemistryMedicineConnective Tissue DiseasesConnective Tissue Disease
Article1 September 1964Serum Sulfhydryl Determinations and Significance in Connective Tissue DiseasesARTHUR LORBER, M.D., CARL M. PEARSON, M.D., F.A.C.P., WROTHER L. MEREDITH, B.A., LOUISE E. GANTZ-MANDELL, B.A.ARTHUR LORBER, M.D.Search for more papers by this author, CARL M. PEARSON, M.D., F.A.C.P.Search for more papers by this author, WROTHER L. MEREDITH, B.A.Search for more papers by this author, LOUISE E. GANTZ-MANDELL, B.A.Search for more papers by this authorAuthor, Article, and Disclosure Informationhttps://doi.org/10.7326/0003-4819-61-3-423 SectionsAboutPDF ToolsAdd to favoritesDownload CitationsTrack CitationsPermissions ShareFacebookTwitterLinkedInRedditEmail ExcerptSulfhydryl (SH) groups are chemically reactive sites located on protein molecules. Oxidation of these groups results in the formation of disulfide bonds (S-S) (1), thereby interlinking the protein molecules and forming macroglobulins. These serum macroglobulins may be dissociated into their protein subunits by thiol (sulfhydryl-containing) compounds that have the ability to break the disulfide bonds (2-5). The importance of sulfhydryl groups in the formation of macroglobulins is further implied by the virtual absence of these groups in the abnormal protein found in Waldenstrom's macroglobulinemia (2) and by the decreased serum sulfhydryl levels reported in other related neoplastic disorders (6).Rheumatoid...References1. WERTHEIM E: Textbook of Organic Chemistry. The Blakiston Company, Philadelphia, 1945, p. 731. Google Scholar2. BLOCHPRASADANATASIBRIGGS HSAADR: Serum protein changes during administration of a low molecular weight thiol (penicillamine). J. Lab. Clin. Med. 56: 212, 1960. Google Scholar3. DEUTSCHMORTON HFJI: Dissociation of human serum macroglobulins. Science 125: 600, 1957. CrossrefMedlineGoogle Scholar4. DEUTSCHMORTON HFJI: Human serum macroglobulins and dissociation units. I. Physico-chemical properties. J. Biol. Chem. 231: 1107, 1958. CrossrefMedlineGoogle Scholar5. PUTNAM FW: Abnormal human serum globulins. Arch. Biochem. 79: 67, 1959. CrossrefGoogle Scholar6. SCHOENBACHWEISSMANARMISTEAD EBNEB: The determination of sulfhydryl groups in serum. II. Protein alterations associated with disease. J. Clin. Invest. 30: 762, 1951. CrossrefMedlineGoogle Scholar7. KUNKEL HG: Studies on the isolation and characterization of the "rheumatoid factor." J. Clin. Invest. 38: 424, 1959. CrossrefMedlineGoogle Scholar8. PLOTZSINGER CMJM: The latex fixation test: results in rheumatoid arthritis. Amer. J. Med. 21: 893, 1956. CrossrefMedlineGoogle Scholar9. ROTHERMICHPHILIPS NOVK: The serological diagnosis of rheumatoid arthritis. JAMA 164: 1999, 1957. CrossrefMedlineGoogle Scholar10. THOMASROBINSONGOFTONSTUCKEYLAMONT-HAVERS JWHSJPMR: The latex fixation test in rheumatoid arthritis. Canad. Med. Ass. J. 76: 621, 1957. MedlineGoogle Scholar11. BENESCHLARDYBENESCH REHAR: The sulfhydryl groups of crystalline proteins. J. Biol. Chem. 216, 663, 1955. CrossrefMedlineGoogle Scholar12. REINHOLD JG: Total protein, albumin, and globulin, in Standard Methods of Clinical Chemistry, edited by REINER, M., Academic Press, Inc., New York, 1963, Vol. 1, p. 88. Google Scholar13. SINGERPLOTZ JMCM: The latex fixation test: application to the serological diagnosis of rheumatoid arthritis. Amer. J. Med. 21: 888, 1956. CrossrefMedlineGoogle Scholar14. JAHNKESCHOLTANHEINZLER KWF: Die visiositat von Serum und isolierten Serum-proteinen bei Makroglobulinamien und anderen Dysund Paraproteinamien. Helv. Med. Acta 25: 2, 1958. MedlineGoogle Scholar15. KUNKEL HG: Macroglobulins and high molecular weight antibodies, in The Plasma Proteins, edited by PUTNAM, F. W., Academic Press, Inc., New York, 1960, Vol. 1, p. 299. CrossrefGoogle Scholar16. Ibid., pp. 302 and 305. Google Scholar17. BAUMSTASTNYZIFF JPM: Effects of the rheumatoid factor and antigen-antibody complexes on the vessels of the rat mesentery. Arthritis Rheum. 5: 101, 1962. Google Scholar18. MCCORMICK JN: An immunofluorescence study of rheumatoid factor. Ann. Rheum. Dis. 22: 1, 1963. CrossrefMedlineGoogle Scholar19. MELLORSNOWOSLAWSKIKORNGOLD RCAL: Rheumatoid arthritis and the cellular origin of rheumatoid factors. Amer. J. Path. 39: 533, 1961. MedlineGoogle Scholar20. MELLORSNOWOSLAWSKIKORNGOLDSENGSON RCALBL: Rheumatoid factor and the pathogenesis of rheumatoid arthritis. J. Exp. Med. 113: 475, 1961. CrossrefMedlineGoogle Scholar21. BALL J: Observations on the presence of rheumatoid serum factor in skin and other tissues. Ann. Rheum. Dis. 21: 272, 1962. CrossrefMedlineGoogle Scholar22. BLANDCLARK JHG: Rheumatoid factor in serum and synovial fluid. Arthritis Rheum. 5: 102, 1962. Google Scholar23. RODNANEISENBEISCRIEGHTON CPCHAS: On the occurrence of rheumatoid factor in synovial fluid. Arthritis Rheum. 5: 316, 1962. Google Scholar24. EDELMANKUNKELFRANKLIN GMHGEC: Interaction of the rheumatoid factor with antigen-antibody complexes and aggregated gamma globulin. J. Exp. Med. 108: 105, 1958. CrossrefMedlineGoogle Scholar25. JANDLENGLEALLEN JHLKDW: Oxodative hemolysis and precipitation of hemoglobin. I. Heinz body anemias as an acceleration of red cell aging. J. Clin. Invest. 39: 1818, 1960. CrossrefMedlineGoogle Scholar26. STEINRAUFDANDLIKER LKWB: A study of the reaction of the disulfide groups of bovine serum albumin during heat denaturation. J. Amer. Chem. Soc. 80: 3833, 1958. CrossrefGoogle Scholar27. LORBER A: Increased globulin fractionation by an improved vertical gel electrophoretic technique. J. Lab. Clin. Med. 64: 133, 1964. MedlineGoogle Scholar28. BOYER PD: Sulfhydryl and disulfide groups of enzymes, in The Enzymes, edited by BOYER, P. D., LARDY, H., MYRBACK, K., Academic Press Inc., New York, 1959, Vol. 1, p. 511. Google Scholar29. RITZMANNBAUGHANLEVIN SEMAWC: In vivo reduction of cold agglutinins by B6-SH. Clin. Res. 11: 34, 1963. Google Scholar30. JAFFE IA: In vivo dissociation of the rheumatoid factor. Arthritis Rheum. 1: 122, 1962. Google Scholar31. JAFFE I: A comparison of the effects of penicillamine and plasmapheresis on the serum. Ann. Rheum. Dis. 22: 71, 1963. CrossrefMedlineGoogle Scholar32. DEUTSCHCHAN HFPC: Human serum hemagglutinins. Fed. Proc. 17: 210, 1958. Google Scholar33. FUDENBERGKUNKEL HHHG: Physical properties of the red cell agglutinins in acquired hemolytic anemia. J. Exp. Med. 106: 689, 1957. CrossrefMedlineGoogle Scholar34. GLENCHURZINNEMANBRIGGS HHHDR: Macroglobulinemia: report of two cases. Arch. Intern. Med. (Chicago) 48: 1055, 1958. LinkGoogle Scholar35. EDELMANNPOULIK GMMD: Studies on structural units of the gamma-globulins. J. Exp. Med. 113: 861, 1961. CrossrefMedlineGoogle Scholar This content is PDF only. To continue reading please click on the PDF icon. Author, Article, and Disclosure InformationAffiliations: Los Angeles, CaliforniaFrom the Departments of Medicine, Wadsworth Veterans Administration Hospital, Sepulveda Veterans Administration Hospital, and the University of California Medical Center, Los Angeles, Calif.This study was supported in part by a grant from the Southern California Chapter of the Arthritis and Rheumatism Association.Request for reprints should be addressed to Arthur Lorber, M.D., Veterans Administration Hospital, Sepulveda, Calif. 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