Linked Life Data

6504215

Source:http://linkedlifedata.com/resource/pubmed/id/6504215

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1985-1-16
pubmed:abstractText
Ascitic fluid of patients with primary liver cancer was shown to contain a latent thiol proteinase which can be activated by pepsin treatment or by autolysis at acidic environment. This enzyme resembles cathepsin B (EC 3.4.22.1) in many physical-chemical properties including substrate specificity, requirement for thiol activators and inhibition both by thiol blocking reagents and by peptidyl diazomethyl ketones, but has a higher molecular size even after activation. Pepsin treatment and autolysis reduce its Mr from 41 800 to 33 400 and 27 700, respectively, but all these forms are larger than human liver cathepsin B. The latent enzyme may be, therefore, an enzyme--inhibitor complex or an inactive precursor of cathepsin B due to an altered processing in Golgi endoplasmatic reticulum-lysosome compartment.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0028-2685
pubmed:author
pubmed:issnType
Print
pubmed:volume
31
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
581-90
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1984
pubmed:articleTitle
Characterization of cathepsin B-like proteinase from ascitic fluid of patients with primary liver cancer.
pubmed:publicationType
Journal Article