Linked Life Data

3524695

Source:http://linkedlifedata.com/resource/pubmed/id/3524695

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1986-9-17
pubmed:abstractText
Some physico-chemical properties of lytic proteinase L2 isolated from the enzymatic microbial preparation of lysoamidase were studied. The molecular mass of the enzyme is 15 000 Da, pI is 5.3. The enzyme hydrolyzes casein as well as the cells and cell walls of Staphylococcus aureus 209-P. The pH optimum of casein hydrolysis lies at 9.5; that for cell wall hydrolysis at 8.0. The temperature optimum for casein hydrolysis and cell lysis lies at 55 degrees C and 65 degrees C, respectively. The enzyme proteolytic activity is inhibited by serine proteinase inhibitors in a greater degree than the lytic activity. 50% of the proteolytic and lytic activities is lost upon enzyme heating for 15 min at 65 degrees C.
pubmed:language
rus
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0320-9725
pubmed:author
pubmed:issnType
Print
pubmed:volume
51
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
909-15
pubmed:dateRevised
2007-7-23
pubmed:meshHeading
pubmed:year
1986
pubmed:articleTitle
[Various physico-chemical properties of lytic proteinase L2 of the enzyme preparation lysoamidase isolated from bacteria of Pseudomonadaceae family].
pubmed:publicationType
Journal Article, English Abstract