Isolation of the liver N-aspartyl-beta-glucosaminidase in aspartylglucosaminuria.

Abstract

The isolation of liver N-aspartyl-beta-glucosaminidase in human aspartylglucosaminuria, where this enzyme activity is diminished, yields an enzyme molecule with the same molecular weight and pH optimum as the normal enzyme. Its activity is 10% of that of the control preparation. Combination of both enzymes results in the summation of both activities, and the pathological enzyme does not inhibit the control preparation. It is concluded that no change into a totally different isoenzyme has occurred in aspartylglucosaminuria.

• Authors: H Savolainen
• Journal: The Biochemical journal (Biochem J) Vol. 153 Issue 3 Pg. 749-50 (Mar 01 1976) ISSN: 0264-6021 [Print] England
• PMID: 942387 (Publication Type: Journal Article)

Chemical References

• Amidohydrolases
• Aspartylglucosylaminase

Topics

• Amidohydrolases (isolation & purification)
• Aspartylglucosaminuria
• Aspartylglucosylaminase (isolation & purification)
• Electrophoresis, Polyacrylamide Gel
• Humans
• Liver (enzymology)