Linked Life Data

7588793

Source:http://linkedlifedata.com/resource/pubmed/id/7588793

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1995-12-18
pubmed:abstractText
Acid cysteine protease was purified from metacercariae of the mammalian trematode parasite Paragonimus westermani. The purified enzyme had a molecular mass of 27 kDa and was a monomeric polypeptide. The protease had an absolute requirement for a reducing agent for full activity towards fluorescein-isothiocyanate-labeled hemoglobin, and it was active in the acidic pH range, with an optimum pH of 4.0. While acidic proteolysis was insensitive to the aspartic protease inhibitor pepstatin A, activity was significantly inhibited by the cysteine protease inhibitors, leupeptin, chymostatin and L-trans-epoxy-succinyl-L-leucylamido(4-guanidino)-butane. The sensitivity of the enzyme to the inhibitors was similar to that of cathepsins B and L, but the specificity of the protease towards chromogenic substrates was slightly different from that of the cathepsins. The purified enzyme was highly specific for N-substituted peptidyl substrates containing arginine in the P1 position and phenylalanine in the P2 position, and the protease extensively degraded human native proteins, such as human serum albumin, immunoglobulins, complement components and also endogenous protease inhibitors. Since the protease hydrolyzes both soluble proteins and components of human defense systems, it may facilitate parasite nutrition and evasion of host defense mechanisms.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0014-2956
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
233
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
490-7
pubmed:dateRevised
2007-7-23
pubmed:meshHeading
pubmed:year
1995
pubmed:articleTitle
Purification and characterization of acid cysteine protease from metacercariae of the mammalian trematode parasite Paragonimus westermani.
pubmed:affiliation
Department of Parasitology, National Defense Medical College, Saitama, Japan.
pubmed:publicationType
Journal Article