Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1988-12-21
pubmed:abstractText
A high molecular weight, fatty acid- and SDS-sensitive protease named ingensin was purified from rat brain in this study. The enzyme purified from rat brain has the same biochemical properties as those purified from other tissues, e.g., porcine skeletal muscle, human placenta, and rat liver in our laboratory, and rat skeletal muscle and bovine pituitary gland in other laboratories, independently. Immunoblot bands were detected in the same positions as those in the case of ingensin from rat liver. In addition, its topographical distribution was studied in rat brain and muscle by means of the immunohistochemical method. The cytoplasm of motor neurons of the spinal cord, pyramidal cells, and granular cells of the hippocampus, Purkinje cells, and glial cells were stained. Axons were stained. The cytoplasm of muscle was also stained, especially that of type 2 fibers.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0360-4012
pubmed:author
pubmed:issnType
Print
pubmed:volume
20
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
473-8
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1988
pubmed:articleTitle
Localization of ingensin in rat central nervous system and skeletal muscle.
pubmed:affiliation
Division of Neuromuscular Research, National Institute of Neuroscience, Tokyo, Japan.
pubmed:publicationType
Journal Article