Faculty Research 1970 - 1979

Title

Purification and chemical properities of mouse liver lysosomal (L form) beta-glucuronidase.

Document Type

Article

Publication Date

1975

Keywords

Animal, Carbohydrates: an, Drug-Stability, Electrophoresis-Polyacrylamide-Gel, Genes-Structural, Glucuronidase: an, ip, Heat, Liver: en, Lysosomes: en, Male, Mice, Mice-Inbred-C57BL, Molecular-Weight, Mutation, SUPPORT-U-S-GOVT-NON-P-H-S, SUPPORT-U-S-GOVT-P-H-S

JAX Source

J Biol Chem 1975 Nov 10; 250(21):8503-9.

Abstract

The lysosomal form (L form) of beta-glucuronidase was purified 6,500-fold from the liver of C57BL/6J mice with high yield. Purified enzyme was homogeneous as judged by polyacrylamide gel electrophoresis in the presence or absence of sodium dodetcyl sulfate. The microsomal forms of beta-glucuronidase were spontaneously converted to the L form. The purified L form is a tetramer of molecular weight of 280,000 to 300,000, composedd of four identical subunits of 75,000 molecular weight. The enzyme contains a high content of arginine and glutamic acid and a very low content of sulfur-containing amino acids. Approximately 7% of the enzyme molecule is compose of carbohydrate. Sugars in the L form are glucosamine, mannose, galactose, and glucose. Sialic acid and fucose are absent in the enzyme.

Please contact the Joan Staats Library for information regarding this document.

Share

COinS