Skip to main content
Biochemical Journal logoLink to Biochemical Journal
. 1973 Nov;135(3):457–462. doi: 10.1042/bj1350457

N-Acetyl-β-d-hexosaminidase component A. Different forms in human tissues and fluids

J Uzoma Ikonne 1, Roland B Ellis 1
PMCID: PMC1165847  PMID: 4359018

Abstract

1. Hexosaminidase A of human serum was resolved into two components, a minor form with properties identical with those of the single hexosaminidase A component of human liver, and a major form with significantly different properties. 2. The major serum hexosaminidase A form was eluted from a DEAE-cellulose column at a lower salt concentration than that required to elute the liver form. 3. A multiple-pass technique was used to elute the major serum enzyme A from a Sephadex G-150 column before that of liver enzyme A. 4. Clostridium perfringens neuraminidase converted the major component of serum hexosaminidase A into a form that was held less tightly by DEAE-cellulose, but the minor component of the A enzyme of serum, and the A enzyme of liver were not affected. 5. The hexosaminidase A from tears was similar to the A enzyme from serum, whereas those from several human tissues and from urine and lymph were similar to the liver form. 6. The A enzyme from serum may be derived from the A enzyme from liver by glycosylation before secretion.

Full text

PDF
457

Selected References

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

  1. Andrews P. The gel-filtration behaviour of proteins related to their molecular weights over a wide range. Biochem J. 1965 Sep;96(3):595–606. doi: 10.1042/bj0960595. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. 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]
  3. Goldstone A., Koenig H. Lysosomal hydrolases as glycoproteins. Life Sci II. 1970 Dec 8;9(23):1341–1350. doi: 10.1016/0024-3205(70)90115-3. [DOI] [PubMed] [Google Scholar]
  4. Goldstone A., Konecny P., Koenig H. Lysosomal hydrolases: Conversion of acidic to basic forms by neuraminidase. FEBS Lett. 1971 Feb 12;13(1):68–72. doi: 10.1016/0014-5793(71)80667-1. [DOI] [PubMed] [Google Scholar]
  5. Hultberg B. N-acetylhexosaminidase activities in Tay-Sachs disease. Lancet. 1969 Nov 29;2(7631):1195–1195. doi: 10.1016/s0140-6736(69)92520-3. [DOI] [PubMed] [Google Scholar]
  6. Kampine J. P., Brady R. O., Kanfer J. N., Feld M., Shapiro D. Diagnosis of gaucher's disease and niemann-pick disease with small samples of venous blood. Science. 1967 Jan 6;155(3758):86–88. doi: 10.1126/science.155.3758.86. [DOI] [PubMed] [Google Scholar]
  7. Macbeth R. A., Bekesi J. G., Sugden E., Bice S. The metabolism of plasma glycoproteins. I. Studies on the rate of incorporation of glucosamine-1-14C into protein-bound hexosamine and N-acetylneuraminic acid in the normal rat. J Biol Chem. 1965 Oct;240(10):3707–3713. [PubMed] [Google Scholar]
  8. Okada S., O'Brien J. S. Tay-Sachs disease: generalized absence of a beta-D-N-acetylhexosaminidase component. Science. 1969 Aug 15;165(3894):698–700. doi: 10.1126/science.165.3894.698. [DOI] [PubMed] [Google Scholar]
  9. PORATH J., BENNICH H. Recycling chromatography. Arch Biochem Biophys. 1962 Sep;Suppl 1:152–156. [PubMed] [Google Scholar]
  10. 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]
  11. ROBINSON G. B., MOLNAR J., WINZLER R. J. BIOSYNTHESIS OF GLYCOPROTEINS. I. INCORPORATION OF GLUCOSAMINE-14C INTO LIVER AND PLASMA PROTEINS OF THE RAT. J Biol Chem. 1964 Apr;239:1134–1141. [PubMed] [Google Scholar]
  12. Robinson D., Stirling J. L. N-Acetyl-beta-glucosaminidases in human spleen. Biochem J. 1968 Apr;107(3):321–327. doi: 10.1042/bj1070321. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Sandhoff K. Auftrennung der Säuger-N-Acetyl-beta-D-hexosaminidase in multiple Formen durch Elektrofokusserung. Hoppe Seylers Z Physiol Chem. 1968 Sep;349(9):1095–1098. [PubMed] [Google Scholar]
  14. Sandhoff K. Variation of beta-N-acetylhexosaminidase-pattern in Tay-Sachs disease. FEBS Lett. 1969 Aug;4(4):351–354. doi: 10.1016/0014-5793(69)80274-7. [DOI] [PubMed] [Google Scholar]
  15. Winterburn P. J., Phelps C. F. The significance of glycosylated proteins. Nature. 1972 Mar 24;236(5343):147–151. doi: 10.1038/236147a0. [DOI] [PubMed] [Google Scholar]
  16. Young E. P., Ellis R. B., Lake B. D., Patrick A. D. Tay-sachs disease and related disorders: Fractionation of brain N-acetyl-beta-hexosaminidase on DEAE-cellulose. FEBS Lett. 1970 Jul 15;9(1):1–4. doi: 10.1016/0014-5793(70)80295-2. [DOI] [PubMed] [Google Scholar]

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

RESOURCES