Skip to main content
NCBI 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
. 1982 Oct;79(20):6225–6228. doi: 10.1073/pnas.79.20.6225

Evidence that a reducible xylosyl-lysine is the protein linkage of dermatan sulfate.

M O Longas, K Meyer
PMCID: PMC347092  PMID: 6815649

Abstract

Dermatan sulfate, purified by standard methods, displayed one spot at the position of the standard after two-dimensional cellulose acetate electrophoresis and was 99% in GalN, 21.5% in sulfate, and 0.6% in protein; Gal and Xyl (2:1) were the only neutral sugars detected. Its glucuronic acid/iduronic acid ratio was 0.15 and its Mr was approximately equal to 16,000. On reaction with 0.4 M NaOH, its reducing group(s) determined as Glc increased by 71% with concomitant separation of protein and polysaccharide and no alteration of the amino acids; when this reaction was repeated in the presence of 0.3 M NaBH4, only 31% of Lys was detected by standard amino acid analysis and none by TLC of the dansylated amino acids; alkaline cleavage in these conditions yielded only 30% of the original Xyl, xylitol, and a ninhydrin-positive substance different from GalN, which had the retention time of xylitol on Affi-Gel 601 and was also obtained from reduction of dermatan sulfate with a 400-eq excess of Na3BH4 in water under conditions that did not cleave the dermatan sulfate-protein bond. The data indicate that a reducible xylosyl-lysine is the protein linkage of dermatan sulfate from calf ligamentum nuchae.

Full text

PDF
6225

Selected References

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

  1. Akiyama F., Seno N. Linkage regions between dermatan polysulfates and peptides. Biochim Biophys Acta. 1981 May 18;674(3):289–296. doi: 10.1016/0304-4165(81)90359-7. [DOI] [PubMed] [Google Scholar]
  2. BITTER T., MUIR H. M. A modified uronic acid carbazole reaction. Anal Biochem. 1962 Oct;4:330–334. doi: 10.1016/0003-2697(62)90095-7. [DOI] [PubMed] [Google Scholar]
  3. Brownlee M., Vlassara H., Cerami A. Measurement of glycosylated amino acids and peptides from urine of diabetic patients using affinity chromatography. Diabetes. 1980 Dec;29(12):1044–1047. doi: 10.2337/diab.29.12.1044. [DOI] [PubMed] [Google Scholar]
  4. Bunn H. F., Higgins P. J. Reaction of monosaccharides with proteins: possible evolutionary significance. Science. 1981 Jul 10;213(4504):222–224. doi: 10.1126/science.12192669. [DOI] [PubMed] [Google Scholar]
  5. DAVIDSON E., HOFFMAN P., LINKER A., MEYER K. The acid mucopolysaccharides of connective tissue. Biochim Biophys Acta. 1956 Sep;21(3):506–518. doi: 10.1016/0006-3002(56)90188-3. [DOI] [PubMed] [Google Scholar]
  6. Elson L. A., Morgan W. T. A colorimetric method for the determination of glucosamine and chondrosamine. Biochem J. 1933;27(6):1824–1828. doi: 10.1042/bj0271824. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Gros C., Labouesse B. Study of the dansylation reaction of amino acids, peptides and proteins. Eur J Biochem. 1969 Feb;7(4):463–470. doi: 10.1111/j.1432-1033.1969.tb19632.x. [DOI] [PubMed] [Google Scholar]
  8. Hata R., Nagai Y. A rapid and micro method for separation of acidic glycosaminoglycans by two-dimensional electrophoresis. Anal Biochem. 1972 Feb;45(2):462–468. doi: 10.1016/0003-2697(72)90208-4. [DOI] [PubMed] [Google Scholar]
  9. Lee Y. C., Johnson G. S., White B., Scocca J. An accelerated system for analysis of neutral sugars in complex carbohydrates. Anal Biochem. 1971 Oct;43(2):640–643. doi: 10.1016/0003-2697(71)90301-0. [DOI] [PubMed] [Google Scholar]
  10. Light N. D., Bailey A. J. Covalent cross-links in collagen. Methods Enzymol. 1982;82(Pt A):360–372. doi: 10.1016/0076-6879(82)82073-9. [DOI] [PubMed] [Google Scholar]
  11. Longas M. O., Meyer K. Sequential hydrolysis of hyaluronate by beta-glucuronidase and beta-N-acetylhexosaminidase. Biochem J. 1981 Aug 1;197(2):275–282. doi: 10.1042/bj1970275. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. MEYER K., RAPPORT M. M. The hydrolysis of chondroitin sulfate by testicular hyaluronidase. Arch Biochem. 1950 Jul;27(2):287–293. [PubMed] [Google Scholar]
  13. PARK J. T., JOHNSON M. J. A submicrodetermination of glucose. J Biol Chem. 1949 Nov;181(1):149–151. [PubMed] [Google Scholar]
  14. Weiner A. M., Platt T., Weber K. Amino-terminal sequence analysis of proteins purified on a nanomole scale by gel electrophoresis. J Biol Chem. 1972 May 25;247(10):3242–3251. [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