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J Skelly

Publications and source records attributed to J Skelly.

24 records · Page 2Linked to original sources
PubMed1979

Analysis of hepatitis B surface antigen components solubilized with Triton X-100.

Three glycoproteins of intact hepatitis B surface antigen (HBsAg) with mol. wt. of 32 000, 30 000 and 28 000 respectively were identified by reaction with 125I-concanavalin A (Con A) after separation by sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE). The antigen was effectively disrupted with Triton X-100 to produce a structure with a sedimentation coefficient of 3.9S. Affinity chromatography of disrupted HBsAg using concanavalin A-Sepharose 4B (Con A-Sepharose) resulted in two fractions. The first contained material which did not bind to the lectin and consisted of a single polypeptide of mol. wt. 64 000. Further studies revealed this component to be serologically identical to serum albumin and to lack any affinity for antibody to HBsAg. A comparison of the tryptic peptide map of this polypeptide with that of purified serum albumin demonstrated identical amino-acid sequences. The second fraction contained material which bound to Con A and contained two polypeptides with mol. wt. of 28000 and 23000 respectively. HBsAg reactivity was associated with this fraction. This procedure allows the prepartion of HBsAg sub-units in milligram quantities for further immunological studies.

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PubMed1978

The labelling of galactose residues in hepatitis B surface antigen glycoprotein.

The 20 to 25 nm particles of hepatitis B surface antigen were purified from the serum of a carrier chimpanzee. Five major polypeptide species were revealed by sodium dodecyl sulphate-polyacrylamide gel electrophoresis. Treatment of the particles with neuraminidase (EC 3.2.1.18) and galactose oxidase (EC 1.1.3.9) followed by reduction with tritiated sodium borohydride labelled galactose residues in a single glycoprotein with an apparent mol. wt. of 28 000. The glycoprotein was not labelled when neuraminidase treatment was omitted, indicating that the galactose residues are in subterminal positions in the oligosaccharide chains. There was no significant incorporation of radiolabel into lipid. The serological activity of the antigen, as measured by a competitive double-antibody radioimmunoprecipitation assay, was not altered by the labelling procedure nor by exposure to neuraminidase alone.

Animals↗
PubMedDate not supplied

Promoting seniors' health--confronting the issue of incontinence.

Incontinence is a demoralizing and costly problem that severely affects the quality of seniors' lives. With the aging Canadian population expected to double within the next 15 years, the elderly are at the highest risk of developing incontinence. It is now recognised that incontinence can be successfully managed, and in many cases, resolved. A survey was conducted with seniors experiencing problems with incontinence who were receiving home care services. Results showed that incontinence has a significant impact on their lives. Seniors tend to mistakenly see the problem as an inevitable factor in the aging process; consequently many hesitate to seek information. In addition, they face barriers to receiving incontinence care that includes knowledge and access to services and resources. Nurses have the potential to take a leading role in reducing the problem of incontinence and in reducing the impact on the lives of seniors. In order to realize this potential, nurses need to be more aware of their attitudes towards incontinence and more informed about conservative treatment options. Some thought needs to be given to the role of the general nurse, and the role of a specialized nurse such as the nurse continence advisor.

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