Enzyme loading of erythrocytes.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 70 ·No. 9 ·1973-09-00 ·Pages 2663-6

Ihler GM, Glew RH, Schnure FW

Abstract

We demonstrated that beta-glucosidase and beta-galactosidase can be trapped inside erythrocytes by rapid hemolysis of the cell in the presence of these enzymes. Enzyme enters only during hemolysis, and optimum uptake occurs within 60 sec. There is no loss in cell number after hemolysis-induced enzyme uptake, and the ghosts have only a slightly increased mean cell volume. Smaller proteins enter more readily than larger proteins, although enzymes with a molecular weight of at least 180,000 can be readily entrapped by erythrocytes. This finding may provide a useful approach to the problem of enzyme replacement in certain diseases, including Gaucher's disease.

MeSH Terms

Animals Catalase/metabolism Cerebrosides Cytochrome c Group/metabolism Enzyme Therapy Enzymes/administration & dosage Erythrocytes/enzymology Escherichia coli/enzymology Galactosidases/metabolism Gaucher Disease/drug therapy Glucose Glucosidases/metabolism Glycoside Hydrolases/administration & dosage,therapeutic use Hemolysis Humans Hypotonic Solutions Immunoglobulins/metabolism Kidney/enzymology Metabolism, Inborn Errors/drug therapy Molecular Weight Phagocytosis Rats Serum Albumin/metabolism Sodium Chloride Sulfur Isotopes

Chemicals

Cerebrosides Cytochrome c Group Enzymes Hypotonic Solutions Immunoglobulins Serum Albumin Sulfur Isotopes Sodium Chloride Catalase Galactosidases Glucosidases Glycoside Hydrolases Glucose

Authors & Affiliations

3 authors, click to expand affiliations / ORCID

Ihler G M

Glew R H

Schnure F W

References (12)

12 references, click to expand

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Article Info

Journal

Proceedings of the National Academy of Sciences of the United States of America

Abbr.

Proc Natl Acad Sci U S A

ISSN

0027-8424

DOI

10.1073/pnas.70.9.2663

Published

1973-09-00

Pages

2663-6

Language

English

Region

United States

NLM ID

7505876

PMCID

PMC427078

Subset

External Links

PubMed source DOI: 10.1073/pnas.70.9.2663 PMC Full Text View journal details

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