Skip to main content
PMC home page
Biochemical Journal logoLink to Biochemical Journal
. 1971 Mar;122(1):101–106. doi: 10.1042/bj1220101

The subunits of chemically treated proteoglycan isolated from bovine nasal cartilage

A Serafini-Fracassini 1, W H Stimson 1, L Floreani 1
PMCID: PMC1176692  PMID: 4256564

Abstract

1. The light fraction of the proteoglycan of bovine nasal cartilage was split by treatment with 0.1m-hydrochloric acid in acetone. The products were separated by gel filtration on 4% agarose and two retarded fractions were detected and isolated. These two fractions were found to have a Stokes radius of 134 and 47 Å respectively, as determined by calibration of the column against proteins of known hydrodynamic volumes. 2. The 47 Å fraction had a protein content of 4% and a glucosamine/galactosamine ratio 1:23. The 134 Å fraction had a protein content of 20% and a glucosamine/galactosamine ratio 1:4.8. 3. The results of the viscometric studies on both fractions suggested that the 134 Å fraction alone exhibited the property of undergoing reversible pH-dependent aggregation with a transition point at pH4.9. 4. It was concluded that these fractions could represent subunits of the native cartilage proteoglycan.

Full text

PDF
101

Images in this article

104-1PLATE 1
on p.104-1

Selected References

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

  1. 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]
  2. Boothroyd B., Napier E. J., Somerfield G. A. The demethylation of griseofulvin by fungi. Biochem J. 1961 Jul;80(1):34–37. doi: 10.1042/bj0800034. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. CECIL R., OGSTON A. G. Determination of sedimentation and diffusion constants of horse-radish peroxidase. Biochem J. 1951 Jun;49(1):105–106. [PubMed] [Google Scholar]
  4. CESSI C., PILIEGO F. The determination of amino sugars in the presence of amino acids and glucose. Biochem J. 1960 Dec;77:508–510. doi: 10.1042/bj0770508. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. EDELHOCH H. The properties of thyroglobulin. I. The effects of alkali. J Biol Chem. 1960 May;235:1326–1334. [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. GERBER B. R., FRANKLIN E. C., SCHUBERT M. Ultracentrifugal fractionation of bovine nasal chondromucoprotein. J Biol Chem. 1960 Oct;235:2870–2875. [PubMed] [Google Scholar]
  8. HAYES J. E., Jr, VELICK S. F. Yeast alcohol dehydrogenase: molecular weight, coenzyme binding, and reaction equilibria. J Biol Chem. 1954 Mar;207(1):225–244. [PubMed] [Google Scholar]
  9. Hascall V. C., Sajdera S. W. Proteinpolysaccharide complex from bovine nasal cartilage. The function of glycoprotein in the formation of aggregates. J Biol Chem. 1969 May 10;244(9):2384–2396. [PubMed] [Google Scholar]
  10. Hoffman P., Mashburn T. A., Jr, Meyer K., Bray B. A. Proteinpolysaccharide of bovine cartilage. I. Extraction and electrophoretic studies. J Biol Chem. 1967 Sep 10;242(17):3799–3804. [PubMed] [Google Scholar]
  11. Hoffman P., Mashburn T. A., Jr, Meyer K. Proteinpolysaccharide of bovine cartilage. II. The relation of keratan sulfate and chondroitin sulfate. J Biol Chem. 1967 Sep 10;242(17):3805–3809. [PubMed] [Google Scholar]
  12. ITZHAKI R. F., GILL D. M. A MICRO-BIURET METHOD FOR ESTIMATING PROTEINS. Anal Biochem. 1964 Dec;9:401–410. doi: 10.1016/0003-2697(64)90200-3. [DOI] [PubMed] [Google Scholar]
  13. Luscombe M., Phelps C. F. The composition and physicochemical properties of bovine nasal-septa protein-polysaccharide complex. Biochem J. 1967 Jan;102(1):110–119. doi: 10.1042/bj1020110. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. MALAWISTA I., SCHUBERT M. Chondromucoprotein: new extraction method and alkaline degradation. J Biol Chem. 1958 Jan;230(1):535–544. [PubMed] [Google Scholar]
  15. MATHEWS M. B., LOZAITYTE I. Sodium chondroitin sulfate-protein complexes of cartilage. I. Molecular weight and shape. Arch Biochem Biophys. 1958 Mar;74(1):158–174. doi: 10.1016/0003-9861(58)90210-8. [DOI] [PubMed] [Google Scholar]
  16. Mathews M. B., Cifonelli J. A. Comparative biochemistry of keratosulfates. J Biol Chem. 1965 Nov;240(11):4140–4145. [PubMed] [Google Scholar]
  17. ROGERS K. S., HELLERMAN L., THOMPSON T. E. L-GLUTAMATE DEHYDROGENASE. 3. MOLECULAR SIZE OF BOVINE GLUTAMATE DEHYDROGENASE AND THE METHYLMERCURIC BROMIDE-ACTIVATED ENZYME IN THE CONCENTRATION RANGE OF ENZYMATIC ASSAY. J Biol Chem. 1965 Jan;240:198–200. [PubMed] [Google Scholar]
  18. Serafini-Fracassini A., Durward J. J., Crawford J. The morphology of the heparin-protein macromolecule and its organization in the mast cell granule. J Ultrastruct Res. 1969 Jul;28(1):131–140. doi: 10.1016/s0022-5320(69)90011-2. [DOI] [PubMed] [Google Scholar]
  19. Serafini-Fracassini A., Peters T. J., Floreani L. The protein-polysaccharide complex of bovine nasal cartilage. Studies on the protein core. Biochem J. 1967 Nov;105(2):569–575. doi: 10.1042/bj1050569. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Serafini-Fracassini A., Smith J. W. Observations on the morphology of the proteinpolysaccharide complex of bovine nasal cartilage and its relationship to collagen. Proc R Soc Lond B Biol Sci. 1966 Oct 11;165(1001):440–449. doi: 10.1098/rspb.1966.0076. [DOI] [PubMed] [Google Scholar]
  21. Serafini-Fracassini A. The protein-polysaccharide complex of bovine nasal cartilage. Studies on the molecular organisation. Biochim Biophys Acta. 1968 Dec 23;170(2):289–300. doi: 10.1016/0304-4165(68)90009-3. [DOI] [PubMed] [Google Scholar]
  22. Smith J. W., Peters T. J., Serafini-Fracassini A. Observations on the distribution of the proteinpolysaccharide complex and collagen in bovine articular cartilage. J Cell Sci. 1967 Mar;2(1):129–136. doi: 10.1242/jcs.2.1.129. [DOI] [PubMed] [Google Scholar]

Articles from Biochemical Journal are provided here courtesy of The Biochemical Society

RESOURCES