Electronic Resource
Oxford, UK
:
Blackwell Publishing Ltd
Journal of neurochemistry
15 (1968), S. 0
ISSN:
1471-4159
Source:
Blackwell Publishing Journal Backfiles 1879-2005
Topics:
Medicine
Notes:
Abstract— 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.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1111/j.1471-4159.1968.tb05907.x
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