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J Bourguignon

Publications and source records attributed to J Bourguignon.

81 records · Page 5Linked to original sources
PubMed1981

A redox function for the Calpha2 domain of IgA immunoglobulin.

IgA1 populations were reduced over a range of dithiothreitol concentrations and the products were examined by sodium dodecyl sulfate polyacrylamide gel electrophoresis and peptide mapping. The study showed that IgA was more resistant to reduction than other immunoglobulin classes (IgG, IgM). SDS-polyacrylamide gel electrophoresis showed that intersubunit bond and H-L bond were the most labile disulfide in polymeric and monomeric IgA, respectively. Peptide mapping revealed that the itrachain disulfide of the C alpha 2 domain was more or equally sensitive to the reduction than H-L and intersubunit bonds. Electrochemical experiments demonstrated that this bond had redox properties and the possibility involving disulfide exchange is discussed.

Chemical Phenomena↗
PubMedDate not supplied

Evaluation of a needle-free intravenous access system.

Needle-stick injuries are one of the most severe hazards faced by nurses today. The most physically and emotionally devastating type of injury is from a needle contaminated with human immunodeficiency virus (HIV), but far more likely to occur is infection with other blood-borne pathogens, especially hepatitis B. The daily threat of needle-stick injuries adds yet another dimension of concern to the stresses inherent in working in a health care facility. Health care workers at greatest risk are those who manipulate needles and draw blood samples on a regular basis. With this concern in mind, a study was launched to evaluate a needle-free I.V. access system with respect to the following research objectives: 1) to assess the prevention/reduction of needle-stick risks and injuries; 2) to identify associated reduction in expenses; 3) to implement product and ease of use; and 4) to assess nursing satisfaction levels. This article describes the methodology used and the results of the study.

Catheters, Indwelling↗
PubMedDate not supplied

[Two new peptic fragments of human IgA: F(abc)'2Alpha and [F(abc)'2]2alpha (author's transl)].

These experiments were undertaken to study the nature of the fragments produced by pepsin digestion of seric IgA. We describe a new fragment with a MW of 140,000 daltons. This fragment, the first produced during pepsin hydrolysis of monomeric IgA, corresponds to an IgA molecule which has lost its CH3 domain. We propose to call this fragment F(abc)'2alpha. It is gradually digested and transformed into an F(ab)'2alpha fragment. When polymeric IgA are digested, an extra fragment with a MW of 290,000 daltons is produced, which has kept its polymeric structure. It corresponds to a covalent [F(abc)'2]2alpha fragment. These findings suggest that there is an intersubunit disulfide bridge in the Calpha2 domain. These results also indicate that polymeric IgA proteins are more resistant to pepsin digestion than monomeric IgA proteins.

Humans↗
PubMedDate not supplied

[Cartilage and vitamin D in vitro (author's transl)].

Interactions between cartilage and vitamin D metabolism were studied in vitro. Chondrocytes were isolated from rabbit growth plate cartilage and cultured. These cells are able to transform 25-hydroxycholecalciferol in 24, 25-dihydroxycholecalciferol. Metabolic transformation is modulated by 1, 25-dihydroxycholecalciferol but not by parathyroid hormone neither by extracellular calcium concentrations. 24, 25-(OH) 2D3 and 1, 25-(OH) 2D3 are active on the cellular metabolism of cultured chondrocytes in a different way : 24, 25-(OH) 2D3 stimulates the proteoglycan synthesis in "mature" chondrocytes 1, 25-(OH) 2D3 increases DNA polymerase activities in chondrocytes during the logarithmic phase of division. Finally, specific sites of nuclear receptors of 24, 25-(OH) 2D3 are present in chondrocytes.

Animals↗