Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
9
pubmed:dateCreated
1973-11-30
pubmed:abstractText
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.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/4354859-10976201, http://linkedlifedata.com/resource/pubmed/commentcorrection/4354859-13575771, http://linkedlifedata.com/resource/pubmed/commentcorrection/4354859-14253443, http://linkedlifedata.com/resource/pubmed/commentcorrection/4354859-14421492, http://linkedlifedata.com/resource/pubmed/commentcorrection/4354859-14907713, http://linkedlifedata.com/resource/pubmed/commentcorrection/4354859-4176481, http://linkedlifedata.com/resource/pubmed/commentcorrection/4354859-4323229, http://linkedlifedata.com/resource/pubmed/commentcorrection/4354859-4718787, http://linkedlifedata.com/resource/pubmed/commentcorrection/4354859-4898857, http://linkedlifedata.com/resource/pubmed/commentcorrection/4354859-5332170, http://linkedlifedata.com/resource/pubmed/commentcorrection/4354859-5477334, http://linkedlifedata.com/resource/pubmed/commentcorrection/4354859-6058309
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Catalase, http://linkedlifedata.com/resource/pubmed/chemical/Cerebrosides, http://linkedlifedata.com/resource/pubmed/chemical/Cytochrome c Group, http://linkedlifedata.com/resource/pubmed/chemical/Enzymes, http://linkedlifedata.com/resource/pubmed/chemical/Galactosidases, http://linkedlifedata.com/resource/pubmed/chemical/Glucose, http://linkedlifedata.com/resource/pubmed/chemical/Glucosidases, http://linkedlifedata.com/resource/pubmed/chemical/Glycoside Hydrolases, http://linkedlifedata.com/resource/pubmed/chemical/Hypotonic Solutions, http://linkedlifedata.com/resource/pubmed/chemical/Immunoglobulins, http://linkedlifedata.com/resource/pubmed/chemical/Serum Albumin, http://linkedlifedata.com/resource/pubmed/chemical/Sodium Chloride, http://linkedlifedata.com/resource/pubmed/chemical/Sulfur Isotopes
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0027-8424
pubmed:author
pubmed:issnType
Print
pubmed:volume
70
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2663-6
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed-meshheading:4354859-Animals, pubmed-meshheading:4354859-Catalase, pubmed-meshheading:4354859-Cerebrosides, pubmed-meshheading:4354859-Cytochrome c Group, pubmed-meshheading:4354859-Enzymes, pubmed-meshheading:4354859-Erythrocytes, pubmed-meshheading:4354859-Escherichia coli, pubmed-meshheading:4354859-Galactosidases, pubmed-meshheading:4354859-Gaucher Disease, pubmed-meshheading:4354859-Glucose, pubmed-meshheading:4354859-Glucosidases, pubmed-meshheading:4354859-Glycoside Hydrolases, pubmed-meshheading:4354859-Hemolysis, pubmed-meshheading:4354859-Humans, pubmed-meshheading:4354859-Hypotonic Solutions, pubmed-meshheading:4354859-Immunoglobulins, pubmed-meshheading:4354859-Kidney, pubmed-meshheading:4354859-Metabolism, Inborn Errors, pubmed-meshheading:4354859-Molecular Weight, pubmed-meshheading:4354859-Phagocytosis, pubmed-meshheading:4354859-Rats, pubmed-meshheading:4354859-Serum Albumin, pubmed-meshheading:4354859-Sodium Chloride, pubmed-meshheading:4354859-Sulfur Isotopes
pubmed:year
1973
pubmed:articleTitle
Enzyme loading of erythrocytes.
pubmed:publicationType
Journal Article