The propeptide of beta-glucuronidase. Further evidence of its involvement in compartmentalization of beta-glucuronidase and sequence similarity with portions of the reactive site region of the serpin superfamily.

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Article

The propeptide of beta-glucuronidase. Further evidence of its involvement in compartmentalization of beta-glucuronidase and sequence similarity with portions of the reactive site region of the serpin superfamily.

The Journal of biological chemistry - 5 Sept 1990

Li H, Takeuchi K H, Manly K, Chapman V, Swank R T

Abstract excerpt

A significant portion of murine hepatocyte beta-glucuronidase is maintained within the endoplasmic reticulum (ER) by complex formation with the esterase active site of the protein egasyn. The carboxyl-terminal propeptide of the precursor form of glucuronidase appears important in localization of glucuronidase to the ER since a naturally occurring mutation in it is associated with decreased levels of ER...

Topics

Amino Acid Sequence
Animals
Base Sequence
Endoplasmic Reticulum
Enzyme Precursors
Glucuronidase
Kidney
Liver
Mice
Mice, Inbred C57BL
Mice, Mutant Strains

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Molecular Sequence Data

Multigene Family

Mutation

Polymerase Chain Reaction

Sequence Homology, Nucleic Acid

Serpins

Source

Open in PubMed

Identifiers

PMID: 2394691

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-2394691-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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