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l ‐A lany ‐β‐NAPHTHYLAMIDASE IN RAT SPINAL CORD MYELIN
Author(s) -
Beck C. S.,
Hasinoff Catherine W.,
Smith Marion E.
Publication year - 1968
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.1471-4159.1968.tb05907.x
Subject(s) - myelin , spinal cord , enzyme , enzyme assay , chemistry , fractionation , biochemistry , specific activity , microbiology and biotechnology , biology , central nervous system , chromatography , endocrinology , neuroscience
— The properties of l ‐alanyl‐β‐naphthylamidase were studied in purified myelin of the spinal cord. The enzyme could be partially extracted with Triton‐X‐100, but some activity was lost by this operation. l ‐Alanyl‐β‐naphthylamidase migrated anodally in acrylamide gel, and the bulk of the activity did not appear to be associated with the basic protein or with the proteolipid protein of myelin. This enzyme is somewhat elevated with acute EAE, but subcellular fractionation of the spinal cord showed that the increased activity was not in the myelin but in the heavier particulate fractions. The relatively small increase in enzyme activity with EAE indicates that this enzyme is probably not a major causative agent in demyelination.