Linked Life Data

16616785

Source:http://linkedlifedata.com/resource/pubmed/id/16616785

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2-3
pubmed:dateCreated
2006-5-8
pubmed:abstractText
A method was developed to separate proteinases in a complex mixture in two dimensions followed by activity detection using class specific substrates. Using this method, serine proteinase activity was evaluated in gut extracts from a stored-product pest, Plodia interpunctella. With the substrate n-alpha-benzoyl-l-arginine rho-nitroanilide, three major groups of at least six trypsin-like activities were identified, consisting of proteinases with estimated molecular masses of 25-27, 40-41, and 289 kDa, and all with an acidic pI of 4.7-5.5. With the substrate, n-succinyl-ala-ala-pro-phenylalanine rho-nitroanilide, two groups of at least five chymotrypsin-like activities were detected, with estimated molecular masses of 28 and 192 kDa and pI values ranging from 6.1 to 7.3. Using the 2-DE activity blot method, information was obtained on the relative number and physical properties of serine proteinases in a mixture of insect gut proteinases without prior fractionation.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0165-022X
pubmed:author
pubmed:issnType
Print
pubmed:day
30
pubmed:volume
67
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
173-9
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2006
pubmed:articleTitle
Two-dimensional analysis of proteinase activity.
pubmed:affiliation
USDA ARS Grain Marketing and Production Research Center, 1515 College Avenue, Manhattan, KS 66502, USA. bso@ksu.edu
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't