Purification and properties of human kidney cortex hexosaminidases A and B

J. E. Wiktorowicz, Y. C. Awasthi, A. Kurosky, S. K. Srivastava

Research output: Contribution to journalArticlepeer-review

34 Scopus citations


Hexosaminidases A and B from human kidney cortex were purified to homogeneity (concanavalin A affinity chromatography, ion-exchange chromatography and gel filtration). The yield of homogeneous isoenzymes improved about 20-fold, giving preparations of hexosaminidases A and B with specific activities of about 200 and 325 units/mg of protein respectively. The kinetic and structural properties of kidney hexosaminidase isoenzymes were studied and compared with the hexosaminidase isoenzymes from human placenta. The amino acid composition of hexosaminidase A was significantly different from that of hexosaminidase B. In the event of success in developing enzyme-replacement therapy for Tay-Sachs and Sandhoff's diseases, this modified procedure can furnish larger amounts of homogeneous isoenzymes.

Original languageEnglish (US)
Pages (from-to)49-53
Number of pages5
JournalBiochemical Journal
Issue number1
StatePublished - 1977
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology


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