Linked Life Data

7063276

Source:http://linkedlifedata.com/resource/pubmed/id/7063276

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1982-5-12
pubmed:abstractText
Biochemical studies on human prolidase (EC 3.4.13.9) and prolidase deficiency are described. The urine sample from a 32-year-old female with prolidase deficiency was examined. Diagnosis was based on clinical features and defects of prolidase in her erythrocytes. She excreted massive amounts of iminopeptides, where three major peptides were identified; aspartyl-proline, glutamyl-proline and glycyl-proline. The prolidase was purified approximately 10,000-fold from the normal human erythrocytes through an eight step procedure. The purified enzyme consisted of two identical subunits of which the molecular weight was calculated to be 55,000. The relative cleavage rates of the enzyme for glycyl-L-proline, L-alanyl-L-proline, L-leucyl-L-proline, L-prolyl-L-proline, and glycyl-hydroxy-L-proline were 100%, 53%, 27%, 31% and 2%, respectively. The relative substrate specificity of the enzyme offers a reasonable explantation for the presence of a higher level of urinary imidodipeptides in a patient with prolidase deficiency. An attempt at erythrocyte transfusion was performed, aimed at enzyme replacement therapy. After the transfusion (erythrocytes from 800 ml of whole blood), the prolidase activity of the peripheral erythrocyte was elevated to approximately 35% of the normal values and gradually decreased (half-life, 41 days). During this period urinary peptide-bound proline was monitored, but no significant change was observed.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0031-3998
pubmed:author
pubmed:issnType
Print
pubmed:volume
16
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
227-31
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1982
pubmed:articleTitle
Human erythrocyte prolidase and prolidase deficiency.
pubmed:publicationType
Journal Article, Case Reports, Research Support, Non-U.S. Gov't