Linked Life Data

1662593

Source:http://linkedlifedata.com/resource/pubmed/id/1662593

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1992-2-20
pubmed:abstractText
1. A serine proteinase isolated from E. superba shows collagenolytic properties: it acts on collagens from Achilles tendon (type I and V) and reconstituted fibrils of calf skin collagen under conditions that do not denature the substrates. 2. At 25 degrees C and pH 7.5 the enzyme both splits the calf skin collagen in solution to the fragments TCA and TCB and catalyses the conversion of dimeric molecules to monomeric chains. 3. The enzyme exhibits strong chymotrypsin-like and lower trypsin-like activities. 4. All the enzyme activities are inhibited to the same degree by diisopropylfluorophosphate (DFP), phenylmethylsulphonyl fluoride (PMSF), N alpha-tosyl-L-lysine chloromethyl ketone (TLCK), soybean trypsin inhibitor (SBTI), chicken ovomucoid (CHOM), chymostatin and leupeptin. None of the activities is inhibited by chelating agents and L-cysteine. 5. pH-Optima of the proteinase in protein substrates hydrolysis (6.0-6.2) are lower than those of synthetic substrates cleavage (7.8-8.0 in the case of BzTyrOEt and 8.7-8.9 for BzArgOEt). 6. Four from nine cysteine residues present in the enzyme molecule possess free thiol-groups. Since the enzyme is inhibited by p-chloromercuribenzoate (pCMB), N-ethylmaleimide (NEM) and iodoacetic acid (IAA), the role of its thiol-groups has been discussed.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0305-0491
pubmed:author
pubmed:issnType
Print
pubmed:volume
99
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
359-71
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1991
pubmed:articleTitle
Collagenolytic serine proteinase from Euphausia superba Dana (Antarctic krill).
pubmed:affiliation
Institute of Technical Biochemistry, Technical University of Lód?, Poland.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't