Abstract：
:The intracellular localization of the serine protease plasminogen activator was analyzed in homogenates of bovine brain cortex using differential fractionation procedures. The distribution of the enzyme was clearly different from that of cytosol and mitochondrial markers, and was similar to that of plasma membrane proteins and of the muscarinic acetylcholine receptor, which is a specific marker for the synaptic membrane. The specific activity of plasminogen activator was increased in fractions enriched in intact synaptosomes. Most of the enzyme in intact synaptosomes was found to be firmly associated with the synaptosomal membrane, and could be solubilized by high concentrations of salt or by non-ionic detergent. Purified synaptic vesicles, however, did not contain large amounts of plasminogen activator. Bovine brain synaptosomes were shown to contain two species of the enzyme, having apparent molecular weights of 80,000 and 55,000. The presence of plasminogen activator in the synaptosomal membrane may indicate its possible involvement in the functioning of nerve terminals.
journal_name
Brain Resjournal_title
Brain researchauthors
Zisapel N,Miskin R,Laudon M,Soreq Hdoi
10.1016/0006-8993(82)91154-4subject
Has Abstractpub_date
1982-09-23 00:00:00pages
129-39issue
1eissn
0006-8993issn
1872-6240pii
0006-8993(82)91154-4journal_volume
248pub_type
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