Purification and characterization of beta -leptinotarsin-h, an activator for presynaptic calcium channel

A new neuroactive protein, beta -leptinotarsin-h, has purified to near-homogeneity from the hemolymph of the beetle Leptinotarsa haldemani by column chromatography. beta -Leptinotarsin-h has a molecular weight of 57000. Rat brain synaptosomes incubated with appropriate radioactive precursors release...

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Bibliographic Details
Published in:Biochemistry (Easton) 1984-01, Vol.23 (4), p.734-740
Main Authors: Crosland, R D, Hsiao, TH, McClure, W O
Format: Article
Language:English
Subjects:
beta -leptinotarsin
calcium
Chrysomelidae
Leptinotarsa haldemani
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Summary:A new neuroactive protein, beta -leptinotarsin-h, has purified to near-homogeneity from the hemolymph of the beetle Leptinotarsa haldemani by column chromatography. beta -Leptinotarsin-h has a molecular weight of 57000. Rat brain synaptosomes incubated with appropriate radioactive precursors release acetylcholine (ACh), norepinephrine, and 4- aminobutyrate when exposed to beta -leptinotarsin-h, but do not release lactate dehydrogenase. Varying the concentration of Ba super(2+), Sr super(2+), Co super(2+), and Cd super(2+) indicates that beta -leptinotarsin-h acts to open the voltage-sensitive presynaptic Ca super(2+) channel. beta -leptinotarsin-h may be a useful tool for studying the Ca super(2+) channel associated with the release of neurotransmitters.
ISSN:0006-2960