Zobrazeno 1 - 10
of 14
pro vyhledávání: '"J R Slemmon"'
Publikováno v:
Molecular neurobiology. 22(1-3)
Neuromodulin (GAP-43), neurogranin (RC3), and PEP-19 are small acid-stable proteins that bind calcium-poor calmodulin through a loosely conserved IQ-motif. Even though these proteins have been known for many years, much about their function in cells
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 108
Publikováno v:
Biopolymers. 43(2)
The use of a method to follow changes in endogenous peptide production, as they occur in biological studies, is an excellent complement to other molecular techniques. It has the unique ability to characterize peptides that have been produced from pro
Autor:
M R Martzen, J R Slemmon
Publikováno v:
Biochemistry. 33(18)
The calmodulin-binding polypeptide neuromodulin (GAP-43) was tested in vitro for its ability to modulate a typical calmodulin target, the enzyme nitric oxide synthase. The titration of enzyme with increasing neuromodulin concentrations demonstrated a
Publikováno v:
Free Radicals in Diagnostic Medicine ISBN: 9781461357421
Several recent studies have reported increased blood-brain barrier (BBB) permeability to large molecules such as immunoglobins and serum albumin following global ischemia.1 These studies have been qualitative, however, using immunohistochemical metho
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::79dd476308aa86e7cdd40cafd316588f
https://doi.org/10.1007/978-1-4615-1833-4_44
https://doi.org/10.1007/978-1-4615-1833-4_44
Publikováno v:
Advances in experimental medicine and biology. 366
Publikováno v:
Journal of Biological Chemistry. 257:3853-3856
The newly developed monoclonal antibody technology was applied to the production of antibodies selective for Drosophila melanogaster choline acetyltransferase (EC 2.3.1.6). Two stable cell lines, 1C8 and 1G4, were isolated from NS-1/spleen cell hybri
Autor:
Eugene Roberts, J R Slemmon, Keiichi Itakura, J E Shively, E Morita, Paul M. Salvaterra, N Itoh, G D Crawford, D H Hawke, R.T. Williamson
Publikováno v:
Proceedings of the National Academy of Sciences. 83:4081-4085
Choline acetyltransferase (EC 2.3.1.6) is the biosynthetic enzyme for the neurotransmitter acetylcholine. To isolate choline acetyltransferase cDNA clones, a cDNA library was constructed from poly(A)+ RNA of Drosophila melanogaster heads, these being
Publikováno v:
Journal of Biological Chemistry. 257:3847-3852
Choline acetyltransferase (EC 2.3.1.6) from Drosophila melanogaster (Canton S, wild type) was purified 12,500-fold to a final specific activity of 500 mumol min-1 mg protein-1. The purification used homogenized fly heads and consisted of polyethylene
Publikováno v:
The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society. 28(1)
The preparation and characterization of a horseradish peroxidase-rabbit antiperoxidase Fab immunocomplex (HRP-Fab2) useful for immunocytochemical localization of primary tissue-bound rabbit antibody are described. Antisera with titer to horseradish p