ALBERT — All Library Books, journals and Electronic Records Telegrafenberg

Hits per page

hits 1 - 2 | 2 hits

Sorting

Electronic Resource

The distribution of cholinergic and adrenergic nerve fibres in the retractor penis and vas deferens of the dog (1970)

Bell, Christopher ; McLean, John R.

Springer

Cell & tissue research 106 (1970), S. 516-522

add to mindlist on the mindlist

Details

ISSN: 1432-0878

Keywords: Retractor penis ; Vas deferens ; Dog ; Autonomic innervation

Source: Springer Online Journal Archives 1860-2000

Topics: Biology , Medicine

Notes: Summary Sections of the retractor penis and vas deferens of the dog have been examined to reveal the histochemical localization of noradrenaline (NA) and acetylcholinesterase (AChE) in the intrinsic nerve fibres. Pine varicose nerves containing NA were abundant along the entire length of the retractor penis muscle, while fine fibres exhibiting high AChE activity were restricted almost entirely to the anterior half of the muscle. In the testicular end of the vas deferens, a dense plexus of noradrenergic nerves was found at the base of the mucosal epithelial cells and other NA-containing nerves were scattered relatively sparsely through the muscle coats. In contrast, at the urethral end, the smooth muscle coats contained a far more dense population of NA-containing nerves, and there was no evidence of a submucosal nerve plexus. Fibres exhibiting high AChE activity were also found throughout the muscle coats, but no concentration of staining fibres was observed in the submucosa at the testicular end of the organ. It is concluded that the smooth muscle of both the retractor penis and the vas deferens of the dog may receive innervation from separate adrenergic and cholinergic fibres. Appreciable levels of AChE do not appear to be associated with adrenergic axons in this species.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1007/BF00340289

Permalink

	Location	Call Number	Expected	Availability

Others were also interested in ...

Paper (German National Licenses)

Fulltext

Electronic Resource

Polypeptide subunits of dynein 1 from sea urchin sperm flagella (1979)

Bell, Christopher W. ; Fronk, Earl ; Gibbons, I. R.

New York, N.Y. : Wiley-Blackwell

Journal of Supramolecular Structure 11 (1979), S. 311-317

add to mindlist on the mindlist

Details

ISSN: 0091-7419

Keywords: dynein ; flagella ; ATPase ; sperm motility ; sea urchin ; Life Sciences ; Molecular Cell Biology

Source: Wiley InterScience Backfile Collection 1832-2000

Topics: Biology , Chemistry and Pharmacology , Medicine

Notes: A high-resolution sodium dodecyl sulfate polyacrylamide gel electrophoresis system has been used to show the presence, in both whole sperm and isolated flagellar axonemes, of eight polypeptides migrating in the 300,000-350,000 molecular weight range characteristic of the heavy chains of dynein ATPase. Previously, only five such chains have been discernible. Extraction of isolated axonemes for 10 min at 4°C with a solution containing 0.6 M NaCl, pH 7, releases a mixture of particles that separate, in sucrose density gradient centrifugation, into a major peak, dynein 1 ATPase, sedimenting at 21 S and a minor peak at 12-14S. The polypeptide compositions of these two peaks are different. The dynein 1 peak, which contains most of the protein on the gradient, contains approximately equal quantities of two closely migrating heavy chains, with a small amount of a third, more slowly migrating chain; no other heavy chains appear in this peak. Two groups of smaller polypeptides (three intermediate chains, within the apparent molecular weight range 76,000-122,000 and four newly discovered light chains, within the apparent molecular weight range 14,000-24,000) cosediment with the 21 S peak. The heavy chain composition of the 12-14S peak is more complex, all eight heavy chains occurring in approximately the same ratios as occur in intact axonemes.

Additional Material: 3 Ill.