Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1975-12-29
pubmed:abstractText
Histochemical investigations of leucine aminopeptidase using LNA (L-leucyl-beta-napthylamide) as a substrate reveals a marked enzyme activity selectively localized to the granular layer with inconspicuous reaction in the stratum moleculare and the Purkinje cells in the rat cerebellum. The LNA-splitting enzyme differs from the well-known leucine aminopeptidase (LAP) by its optimum at pH 5.5. The necessary long incubation period used in the present study, and its focal precipitation of the enzyme reaction product in the same place, like acid phosphatases, in the granular layer, suggest a lysosomal localization. The functional role of the LNA-splitting enzyme has been discussed; it is considered that it is involved not only in the protein transformation for synaptic function, but may perhaps also play an important pathogenic role in necrosis, atrophy or even autolysis.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0365-4184
pubmed:author
pubmed:issnType
Print
pubmed:volume
83
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
503-10
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1975
pubmed:articleTitle
Histochemical demonstration of an LNA-splitting enzyme in the cerebellum of the rat. A aminopeptidase-like reaction localized selectively in the granular layer with acid pH optimum.
pubmed:publicationType
Journal Article