1,721,088 research outputs found
Presenza nel sistema nervoso dei vertebrati inferiori di proteine immunologicamente correlate con i neurofilamenti di mammifero.
No full text9+0" immotile spermatozoa in an infertile man
No full text“9 + 0”‐unbewegliche Spermatozoen bei einem unfruchtbaren Mann Bericht über eine eigene Beobachtung bei einem 27jährigen Mann, der kinderlos verheiratet ist. Die morphologische Untersuchung des Ejakulates ergab normalkonfigurierte Köpfe, allerdings waren die Spermatozoen sämtlich starr und unbeweglich. Alle Spermatozoen waren normal strukturiert mit dem überall vorhandenen Charakteristikum, daß ein Fehlen der Zentraltubuli und der Fortsätze, welche die sog. zentrale Scheide bilden, festgestellt ist. Die elektrophoretische Analyse der hochmolekularen Polypeptidketten, die dem Dynein zugeordnet werden, zeigte das konstante Fehlen einer Kette. Die Bedeutung der zentralen Strukturen, im allgemeinen zugehörig zum “9 + 2” Spermatozoon und die mögliche Lokalisation der Dynein‐Kette in dieser Gegend wird auführlich diskutiert. 1979 Blackwell Verlag Gmb
HMW polypeptides from fish neurofilaments cross-react with mammalian NF-H and NF-M subunits.
No full textPorin is bound into a disulfide-stabilized supramolecular assembly in mammalian sperm mitochondria
No full textEvolutionary trends of neurofilament proteins in fish
No full text1. 1. Neurofilament complement was studied in an early chordate (Ciona intestinalis) and six fish species by immunoblot with antisera specific for each of the three mammalian NF subunits. 2. 2. The anti-NF-H and anti-NF-M antisera were characterized as strict for phosphorylated epitopes located in the carboxyterminal domain 3. 3. The NF-L subunit is absent in primitive chordates and appears first in fish; it can be identified on the basis of its apparent mol. wt, its reactivity with the anti-IFA antibody and with polyclonal antibodies raised to the NF-L subunit of mammals. 4. 4. Primitive chordate neurofilaments are constituted by a single polypeptide of ca 160,000 mol. wt exhibiting only M-type phosphorylation-dependent epitopes. 5. 5. Primitive fish (Acipenser transmontanus, Salmo gairdneri, Scorpaena porcus, Serranus scriba) possess only a single high mol. wt NF subunit reacting with both anti-NF-H and anti-NF-M antiserum while more recent species (Mugil saliens, Perca Fluviatilis) possess two high mol. wt NF subunits which are immunologically distinct as to their phosphorylation structures. 6. 6. The existence in some fish species of two high mol. wt NF polypeptides suggests that the process of gene duplication and diversification supposed to have given rise to the two high mol. wt NF subunits of mammals and birds has occurred repeatedly in vertebrate evolution, and may be regarded as a case of convergent evolution. © 1991
Single step purification of a synthetic peptide fragment of neurofilaments by preparative high performance liquid-chromatography
No full textIt was recently shown that fragment Lys-Ser-Pro-Val (1,2) is the major site in vivo neurofilament phosforilation. A suitable method for the preparation of this peptide was therefore studied paying particular attention to the purification step. Even thought solubility of this peptide in methyl t-butil ether does not allow the standard purification. It is possible achieve a good separation in a single step by HPLC, after a simple extraction with acidic water.It was recently shown that fragment Lys-Ser-Pro-Val (1,2) is the major site in vivo neurofilament phosforilation. A suitable method for the preparation of this peptide was therefore studied paying particular attention to the purification step. Even thought solubility of this peptide in methyl t-butil ether does not allow the standard purification. It is possible achieve a good separation in a single step by HPLC, after a simple extraction with acidic water. © 1989, Taylor & Francis Group, LLC. All rights reserved
Immunoblotting bidimensionale dei prodotti di modificazione da antibiotici delle proteine plasmatiche
No full textTwo-dimensional gel electrophoresis of Caenorhabditis elegans homogenates and identification of protein spots by microsequencing
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