Selective calcium-alkali metal exchange in a synaptic membrane protein

1974 ◽  
Vol 30 (2) ◽  
pp. 180-182
Author(s):  
L. G. Abood ◽  
W. Hoss
Keyword(s):  
Membrane Protein ◽  
Alkali Metal ◽  
Synaptic Membrane ◽  
Metal Exchange

scholarly journals The metabolism of neuropeptides. Phase separation of synaptic membrane preparations with Triton X-114 reveals the presence of aminopeptidase N

1985 ◽  
Vol 231 (2) ◽  
pp. 445-449 ◽  
Author(s):  
R Matsas ◽  
S L Stephenson ◽  
J Hryszko ◽  
A J Kenny ◽  
A J Turner
Keyword(s):  
Phase Separation ◽  
Membrane Protein ◽  
Total Activity ◽  
Aminopeptidase N ◽  
The Other ◽  
Aminopeptidase Activity ◽  
Synaptic Membranes ◽  
Synaptic Membrane ◽  
Rich Phase ◽  
Triton X

The property of solutions of Triton X-114 to separate into detergent-rich and detergent-poor phases at 30 degrees C has been exploited to investigate the identities of the aminopeptidases in synaptic membrane preparations from pig striatum. When titrated with an antiserum to aminopeptidase N (EC 3.4.11.2), synaptic membranes solubilized with Triton X-100 revealed that this enzyme apparently comprises no more than 5% of the activity releasing tyrosine from [Leu]enkephalin. When assayed in the presence of puromycin, this proportion increased to 20%. Three integral membrane proteins were fractionated by phase separation in Triton X-114. Aminopeptidase activity, endopeptidase-24.11 and peptidyl dipeptidase A partitioned predominantly into the detergent-rich phase when kidney microvillar membranes were so treated. However, only 5.5% of synaptic membrane aminopeptidase activity partitioned into this phase, although the other peptidases behaved predictably. About half of the aminopeptidase activity in the detergent-rich phase could now be titrated with the antiserum, showing that aminopeptidase N is an integral membrane protein of this preparation. Three aminopeptidase inhibitors were investigated for their ability to discriminate between the different activities revealed by these experiments. Although amastatin was the most potent (IC50 = 5 × 10(−7) M) it failed to discriminate between pure kidney aminopeptidase N, the total activity of solubilized synaptic membranes and that in the Triton X-114-rich phase. Bestatin was slightly more potent for total activity (IC50 = 6.3 × 10(−6) M) than for the other two forms (IC50 = 1.6 × 10(−5) M). Puromycin was a weak inhibitor, but was more selective. The activity of solubilized membranes was more sensitive (IC50 = 1.6 × 10(−5) M) than that of the pure enzyme or the Triton X-114-rich phase (IC50 = 4 × 10(−4) M). We suggest that the puromycin-sensitive aminopeptidase activity that predominates in crude synaptic membrane preparations may be a cytosolic contaminant or peripheral membrane protein rather than an integral membrane component. Aminopeptidase N may contribute to the extracellular metabolism of enkephalin and other susceptible neuropeptides in the brain.

Synaptic membrane protein D2 in the cerebrospinal fluid of manic-melancholic patients

1977 ◽  
Vol 56 (1) ◽  
pp. 50-56 ◽  
Author(s):  
O. S. Jørgensen ◽  
E. Bock ◽  
P. Bech ◽  
O. J. Rafaelsen
Keyword(s):  
Cerebrospinal Fluid ◽  
Membrane Protein ◽  
Synaptic Membrane

scholarly journals Stochastic lattice model of synaptic membrane protein domains

2017 ◽  
Vol 95 (5) ◽  
Author(s):  
Yiwei Li ◽  
Osman Kahraman ◽  
Christoph A. Haselwandter
Keyword(s):  
Membrane Protein ◽  
Lattice Model ◽  
Protein Domains ◽  
Synaptic Membrane

Intercalation materials for secondary batteries based on alkali metal exchange: developments and perspectives

2020 ◽  
Vol 8 (33) ◽  
pp. 16854-16883
Author(s):  
Christian Heubner ◽  
Tobias Lein ◽  
Michael Schneider ◽  
Alexander Michaelis
Keyword(s):  
Alkali Metal ◽  
Metal Exchange ◽  
Intercalation Materials

This review highlights recent insights into and perspectives on intercalation materials for secondary batteries based on alkali-metal exchange techniques.

Immunochemical and immunohistochemical characterization of a synaptic membrane protein that binds the competitive antagonists of NMDA receptors

1993 ◽  
Vol 158 (2) ◽  
pp. 173-176 ◽  
Author(s):  
K.T. Eggeman ◽  
R. Pal ◽  
J. Walsh ◽  
K.N. Kumar ◽  
E.K. Michaelis
Keyword(s):  
Membrane Protein ◽  
Nmda Receptors ◽  
Synaptic Membrane

Nesca, a novel neuronal adapter protein, links the molecular motor kinesin with the pre-synaptic membrane protein, syntaxin-1, in hippocampal neurons

2012 ◽  
Vol 121 (6) ◽  
pp. 861-880 ◽  
Author(s):  
James I. S. MacDonald ◽  
Alfonso Dietrich ◽  
Sarah Gamble ◽  
Todd Hryciw ◽  
Robert Ian Grant ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Hippocampal Neurons ◽  
Molecular Motor ◽  
Synaptic Membrane ◽  
Adapter Protein
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