TY - JOUR
T1 - 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.
AU - Albrechtsen, R
AU - Jensen, H
N1 - Keywords: Animals; Cerebellum; Hydrogen-Ion Concentration; Kidney Cortex; Kidney Tubules; Leucyl Aminopeptidase; Leucyl-beta-Naphthylamidase; Purkinje Cells; Rats; Time Factors
PY - 1975
Y1 - 1975
N2 - 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.
AB - 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.
M3 - Journal article
C2 - 241202
SN - 0365-4184
VL - 83
SP - 503
EP - 510
JO - Acta pathologica et microbiologica Scandinavica. Section A, Pathology
JF - Acta pathologica et microbiologica Scandinavica. Section A, Pathology
IS - 5
ER -