Linked Life Data

7417458

Source:http://linkedlifedata.com/resource/pubmed/id/7417458

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1980-12-18
pubmed:abstractText
Histidine decarboxylase (L-histidine carboxy-lyase, EC 4.1.1.22) of an extract of rat stomach was inactivated by a pancreatic extract. This inactivation was prevented by the protease inhibitors leupeptin, antipan, chymostatin, pepstatin, Trasylol and phenylmethanesulfonyl fluoride. Leupeptin, antipain, chymostatin and pepstatin together and phenylmethanesulfonyl fluoride alone prevented complete inactivation of the enzyme, while Trasylol had a weak protective effect. The inactivation and protection of histidine decarboxylase purified from whole fetal rats were similar to those of the stomach enzyme: both enzymes were strongly inactivated by trypsin and chymotrypsin, but not by elatase or carboxypeptidase Y. The histidine decarboxylase activities of various rat tissues were assayed in the presence of protease inhibitors: activity was highest in mast cells followed by the whole bodies of fetal rats and the stomach, while the activities were lower in decreasing order in the brain, spleen, lung and liver. Heart and kidney had no activity.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:volume
615
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
458-64
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1980
pubmed:articleTitle
The effects of protease inhibitors on histidine decarboxylase activities and assay of enzyme in various rat tissues.
pubmed:publicationType
Journal Article