Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
12
pubmed:dateCreated
1981-9-15
pubmed:abstractText
Thiaminase (EC 2.5.1.2) from freshwater bivalve molluscs is a polycosubstrate enzyme, which is resistant to temperatures below 55 degrees. The activation energy of the enzyme with cystein is 15077 cal/mole, with aniline--15948 cal/mole. Thiaminase when injected parenterally to albino mice 2 hrs after injection of [2-14C]thiamine causes an extensive destruction of labelled vitamin b1, which is evidenced from the [14C]thiazole content in urine, liver and kidneys. The total radioactivity and the content of [14C]thiazole in the urine samples collected within 6 hrs after thiamine injection are increased. Cysteine and histidine in combination with thiaminase have no activating effect similar to that observed "in vitro". In the experimental series when non-labelled vitamin B1 from animal tissues (liver, kidney, spleen, muscle) was substituted by the labelled one, the parenterally injected enzyme destroyed up to 30-50% of total thiamine content. Brain and skeletal muscle tissues are more resistant to thiaminase action.
pubmed:language
rus
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0320-9725
pubmed:author
pubmed:issnType
Print
pubmed:volume
45
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2146-52
pubmed:dateRevised
2007-7-23
pubmed:meshHeading
pubmed:year
1980
pubmed:articleTitle
[Direct measurement of the antivitamin action of parenterally injected thiaminase].
pubmed:publicationType
Journal Article, English Abstract