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At least 505 records · Page 28Linked to original sources
PubMed1971

The fine structural localization of cholinesterases in the carotid body of the cat.

1. The distribution of cholinesterases in the carotid body of the cat has been investigated with the electron microscope to obtain a clearer picture of the localization of the enzyme. This is of relevance to the possible role of acetylcholine as a transmitter in the carotid body.2. Tissues were fixed for short periods and incubated by the method of Karnovsky for the fine localization of cholinesterases.3. The enzyme was found in two main sites. Butyrylcholinesterase was present on the type II cell membrane while acetylcholinesterase was found in groups of peripheral axons. No intracellular enzyme was found.4. It is concluded that acetylcholine may be a transmitter in the carotid body and that it may be partly destroyed by enzymic hydrolysis. A possible explanation for some of the anomalous pharmacological findings is suggested.

Acetylcholine↗
PubMed1968

Tetanus toxin: fine structure localization of binding sites in striated muscle.

When striated muscle from mice poisoned with purified tetanus neurotoxin was incubated with tetanus antitoxin labeled with horseradish peroxidase and stained for peroxidase activity, an electron-opaque reaction product was found in the transverse and terminal sacs of the longitudinal elements of the sarcotubular system. Demonstration of toxin in this location suggests that it acts by interfering with contraction coupling or mechanisms of contraction-relaxation.

Animals↗
PubMed1989

Use of Ar+ plasma etching to localize structural proteins in the capsid of herpes simplex virus type 1.

Partially cored herpes simplex virus type 1 (HSV-1) capsids (B capsids) were eroded in a low-energy (0.5-keV) Ar+ ion plasma under conditions in which the outermost structural proteins were expected to be degraded before more internal ones. After various periods of etching, the proteins remaining intact were separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and determined quantitatively by densitometric scanning of the stained gels. The results showed that the major capsid polypeptide (VP5) and two other capsid proteins, VP19 and VP23, were degraded rapidly beginning as soon as capsids were exposed to the ion plasma. In contrast, significant lags were observed for erosion of VP21, VP22a, and VP24, suggesting that these proteins were available to accelerated ions only after other, more external structures had been damaged or eroded away. The results suggest that VP5, VP19, and VP23 are exposed on the surface of the capsid, while VP21, VP22a, and VP24 are found inside the capsid cavity. The experiments are consistent with the view that VP5 constitutes the major structural component of the hexavalent capsomers. It is proposed that VP19 and VP23 may form other surface structures such as the pentavalent capsomers, the capsid floor, or the intercapsomeric fibers.

Animals↗
PubMed1981

Sex vesicle-associated nucleolar organizers in mouse spermatocytes: localization, structure, and function.

Selective silver staining demonstrated that autosomal bivalents containing transcriptively active nucleolar organizers associated with the sex vesicle during pachytene of mouse spermatocytes. Later in pachytene, the nucleolar organizers covered the portion of the sex vesicle furthest from the attachment to the nuclear envelope. Hybridization in situ revealed the presence of rDNA in the silver-positive material. The nucleolus, formed from an autosomal bivalent, exhibited a large fibrillar center surrounded by an electron-opaque fibrillar zone. The nucleolar association with the sex vesicle was studied at early, middle, and late pachytene by hybridization in situ, NOR silver staining, and electron microscopy. These observations enabled us to further define the relationships of the nucleolar components with the X-Y pair.

Animals↗