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. 1978 Jul 1;173(1):191–196. doi: 10.1042/bj1730191

Characterization of proteins structurally related to human N-acetyl-beta-D-glucosaminidase.

M Carroll
PMCID: PMC1185762  PMID: 99143

Abstract

Those proteins of human liver that cross-reacted with antibodies raised to apparently homogenous hexosamindases A and B were detected by immunodiffusion. Cross-reacting proteins with high molecular weights (greater than 2000000) and intermediate molecular weights (70000--200000) were present both in the unadsorbed fraction and in the 0.05--0.2M-NaCl eluate obtained by DEAE-cellulose chromatography at pH7.0. The unadsorbed fraction also contained a cross-reacting protein of low molecular weight (10000--70000). The possible structural and functional relationships between hexosaminidase and the cross-reacting proteins are discussed. An apparently cross-reacting protein present in the 0.05M-NaCl eluate from the DEAE-cellulose column was serologically unrelated to hexosaminidase, but it gave a reaction of immunological identify with one of the apparently cross-reacting proteins having the charge and size characteristics of hexosaminidase A. It is suggested that immunochemical methods may provide criteria for the homogeneity of enzyme preparations superior to those of conventional methods.

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Selected References

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

  1. Beutler E., Kuhl W., Comings D. Hexosaminidase isozyme in type O Gm2 gangliosidosis (Sandhoff-Jatzkewitz disease). Am J Hum Genet. 1975 Sep;27(5):628–638. [PMC free article] [PubMed] [Google Scholar]
  2. Beutler E., Kuhl W. Subunit structure of human hexosaminidase verified: interconvertibility of hexosaminidase isozymes. Nature. 1975 Nov 20;258(5532):262–264. doi: 10.1038/258262a0. [DOI] [PubMed] [Google Scholar]
  3. Beutler E., Srivastava S. K. Studies in Tay-Sachs and Sandhoff's diseases. Immunologic and structural properties of hexosaminidase A and hexosaminidase B. Isr J Med Sci. 1973 Sep-Oct;9(9):1335–1337. [PubMed] [Google Scholar]
  4. Braidman I., Carroll M., Dance N., Robinson D. Separation and properties of human brain hexosaminidase C. Biochem J. 1974 Nov;143(2):295–301. doi: 10.1042/bj1430295. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Brew K., Vanaman T. C., Hill R. L. The role of alpha-lactalbumin and the A protein in lactose synthetase: a unique mechanism for the control of a biological reaction. Proc Natl Acad Sci U S A. 1968 Feb;59(2):491–497. doi: 10.1073/pnas.59.2.491. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Carroll M., Robinson D. A low-molecular-weight protein cross-reacting with human liver N-acetyl-beta-D-glucosaminidase. Biochem J. 1974 Feb;137(2):217–221. doi: 10.1042/bj1370217. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Carroll M., Robinson D. Immunological properties of N-acetyl-beta-D-glucosaminidase of normal human liver and of GM2-gangliosidosis liver. Biochem J. 1973 Jan;131(1):91–96. doi: 10.1042/bj1310091. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Dingle J. T., Barrett A. J., Weston P. D. Cathepsin D. Characteristics of immunoinhibition and the confirmation of a role in cartilage breakdown. Biochem J. 1971 Jun;123(1):1–13. doi: 10.1042/bj1230001. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Dorfman A., Matalon R. The mucopolysaccharidoses (a review). Proc Natl Acad Sci U S A. 1976 Feb;73(2):630–637. doi: 10.1073/pnas.73.2.630. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Geiger B., Arnon R. Chemical characterization and subunit structure of human N-acetylhexosaminidases A and B. Biochemistry. 1976 Aug 10;15(16):3484–3493. doi: 10.1021/bi00661a014. [DOI] [PubMed] [Google Scholar]
  11. Neufeld E. F., Lim T. W., Shapiro L. J. Inherited disorders of lysosomal metabolism. Annu Rev Biochem. 1975;44:357–376. doi: 10.1146/annurev.bi.44.070175.002041. [DOI] [PubMed] [Google Scholar]
  12. Neuwelt E., Stumpf D., Austin J., Kohler P. A monospecific antibody to human sulfatase A. Preparation, characterization and significance. Biochim Biophys Acta. 1971 Apr 27;236(1):333–346. doi: 10.1016/0005-2795(71)90182-6. [DOI] [PubMed] [Google Scholar]
  13. O'Brien J. S. Tay-Sachs disease: from enzyme to prevention. Fed Proc. 1973 Feb;32(2):191–199. [PubMed] [Google Scholar]
  15. Phillips N., Robinson D., Winchester B. Immunological characterization of human liver alpha-D-mannosidase. Biochem J. 1975 Dec;151(3):469–475. doi: 10.1042/bj1510469a. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Price R. G., Dance N. The demonstration of multiple heat stable forms of N-acetyl- -glucosaminidase in normal human serum. Biochim Biophys Acta. 1972 Jun 22;271(1):145–153. doi: 10.1016/0005-2795(72)90142-0. [DOI] [PubMed] [Google Scholar]
  17. Robinson D., Carrol M., Stirling J. L. Identification of a possible subunit of hexosaminidase A and B. Nature. 1973 Jun 15;243(5407):415–416. doi: 10.1038/243415a0. [DOI] [PubMed] [Google Scholar]
  18. Robinson D., Carroll M. Tay-Sachs disease: interrelation of hexosaminidases A and B. Lancet. 1972 Feb 5;1(7745):322–323. doi: 10.1016/s0140-6736(72)90332-7. [DOI] [PubMed] [Google Scholar]
  19. Sandhoff K., Wässle W. Anreicherung und Charakterisierung zweier Formen der menschlichen N-acetyl- -D-hexosaminidase. Hoppe Seylers Z Physiol Chem. 1971 Aug;352(8):1119–1133. [PubMed] [Google Scholar]
  20. Srivastava S. K., Awasthi Y. C., Yoshida A., Beutler E. Studies on human beta-D-N-acetylhexosaminidases. I. Purification and properties. J Biol Chem. 1974 Apr 10;249(7):2043–2048. [PubMed] [Google Scholar]
  21. Srivastava S. K., Beutler E. Antibody against purified human hexosaminidase B cross-reacting with human hexosaminidase A. Biochem Biophys Res Commun. 1972 May 26;47(4):753–759. doi: 10.1016/0006-291x(72)90556-6. [DOI] [PubMed] [Google Scholar]
  22. Srivastava S. K., Beutler E. Hexosaminidase-A and hexosaminidase-B: studies in Tay-Sachs' and Sandhoff's disease. Nature. 1973 Feb 16;241(5390):463–463. doi: 10.1038/241463a0. [DOI] [PubMed] [Google Scholar]
  23. Srivastava S. K., Beutler E. Studies on human beta-D-N-acetylhexosaminidases. 3. Biochemical genetics of Tay-Sachs and Sandhoff's diseases. J Biol Chem. 1974 Apr 10;249(7):2054–2057. [PubMed] [Google Scholar]
  24. Srivastava S. K., Wiktorowicz J., Klebe R., Awasthi Y. C. Studies on beta-D-N-acetylhexosaminidase. Various isozymes in tissues of normal subjects and Sandhoff's disease patients. Biochim Biophys Acta. 1975 Aug 26;397(2):428–436. doi: 10.1016/0005-2744(75)90132-1. [DOI] [PubMed] [Google Scholar]
  25. Srivastava S. K., Yoshida A., Awasthi Y. C., Beutler E. Studies on human beta-D-N-acetylhexosaminidases. II. Kinetic and structural properties. J Biol Chem. 1974 Apr 10;249(7):2049–2053. [PubMed] [Google Scholar]
  26. Stirling J. L. Human N-acetyl-beta-hexosaminidases: hydrolysis of N, N' diacetylchitobiose by a low molecular weight enzyme. FEBS Lett. 1974 Feb 15;39(2):171–175. doi: 10.1016/0014-5793(74)80044-x. [DOI] [PubMed] [Google Scholar]
  27. Truffa-Bachi P., Guiso N., Cohen G. N., Theze J., Burr B. Evolution of biosynthetic pathways: immunological approach. Proc Natl Acad Sci U S A. 1975 Apr;72(4):1268–1271. doi: 10.1073/pnas.72.4.1268. [DOI] [PMC free article] [PubMed] [Google Scholar]
  28. Van Hoof F., Hue L., De Barsy T., Jacquemin P., Devos P., Hers H. G. Glycogen storage diseases. Biochimie. 1972;54(5):745–752. doi: 10.1016/s0300-9084(72)80177-9. [DOI] [PubMed] [Google Scholar]
  29. Weston P. D. A specific antiserum to lysosomal cathepsin D. Immunology. 1969 Sep;17(3):421–428. [PMC free article] [PubMed] [Google Scholar]

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