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THE QUANTITATIVE HISTOCHEMISTRY OF ACID PROTEINASE IN THE NERVOUS SYSTEM: LOCALIZATION IN NEURONS 1
Author(s) -
Hirsch Hilde E.,
Parks Mary Ellen
Publication year - 1973
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1973.tb04265.x
Subject(s) - neuropil , cerebellum , anterior horn cell , spinal cord , cathepsin , granular layer , nervous system , biology , central nervous system , cathepsin d , nervous tissue , immunohistochemistry , cell bodies , anatomy , biochemistry , microbiology and biotechnology , chemistry , neuroscience , pathology , enzyme , medicine , disease , amyotrophic lateral sclerosis , immunology
A new, fluorometric method was used to assay acid proteinase in tissue samples at great sensitivity. Digestion of hemoglobin at pH 3.8 (in brain mostly due to cathepsin D) was measured in individual nerve cell bodies and neuropil from the anterior horn of the spinal cord, and in the molecular and granular layers and while matter of cerebellum, in man and in monkey. Anterior horn cell perikarya were about 25 times more active than neuropil, and the granular layer of cerebellum had about three times the activity of the molecular layer. This predominantly neuronal localization resembles the distribution of other lysosomal hydrolases. The high capacity for protein breakdown found in neurons is in accord with their known high rates of protein synthesis and turnover.