Purification and properties of human kidney cortex hexosaminidases A and B

J. E. Wiktorowicz, Y. C. Awasthi, A. Kurosky, Satish Srivastava

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Abstract

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
Volume165
Issue number1
StatePublished - 1977

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ASJC Scopus subject areas

  • Biochemistry

Cite this

Wiktorowicz, J. E., Awasthi, Y. C., Kurosky, A., & Srivastava, S. (1977). Purification and properties of human kidney cortex hexosaminidases A and B. Biochemical Journal, 165(1), 49-53.