Linked Life Data

6338188

Source:http://linkedlifedata.com/resource/pubmed/id/6338188

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1983-4-21
pubmed:abstractText
The acid proteases, cathepsin B, dipeptidyl aminopeptidase I and II were demonstrated by fluorescent histochemistry in adult Schistosoma mansoni and Schistosoma japonicum. Alanyl- and leucine-aminopeptidase activities were not observed. The substrates consisted of 4-methoxy-beta-naphthylamide derivatives coupled to the fluorescent molecule, 5-nitrosalicylaldehyde. Reaction product was observed as discrete granules in the gastrodermis; activity was also observed in the testes and vitelline cells of males and females, respectively. No activity was noted in the foregut or esophageal glands of either worm. In light of previous biochemical studies on "hemoglobinase" activity in the schistosomes, it appears likely that a group of acid proteases may be involved in the ultimate digestion of hemoglobin. The absence of activity in the esophageal glands lends further support to the hypothesis that the gastrodermis is the site of the proteases responsible for hemoglobin digestion.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0022-3395
pubmed:author
pubmed:issnType
Print
pubmed:volume
69
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
106-10
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1983
pubmed:articleTitle
Fluorescent histochemistry of acid proteases in adult Schistosoma mansoni and Schistosoma japonicum.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't