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Biomedical subjects

J Jenkins

Publications and source records attributed to J Jenkins.

At least 217 records · Page 12Linked to original sources
PubMed1979

Engagement in activities by old people in residential care.

A major task facing the staff of residential homes for the elderly and of geriatric hospitals is to organise the environment so that the best interests of the elderly residents are met. Such organisation will assist each resident to solve particular problems or to meet the therapeutic goals for which the person was admitted. In addition, and equally important, staff will arrange the day-to-day environment to ensure that all residents have the opportunity to engage in a wide range of activities in order to maintain those abilities they possessed upon admission, together with their health and their interest in life. Ideally, too, the staff will include each resident in the deliberations and decisions about his or her therapeutic goals, and will involve all residents in planning their chosen activities or in making changes to encourage greater participation in the activities available.

Activities of Daily Living↗
PubMed1979

Sinusoidal heart rate rhythms in severe neonatal hypoxia.

Sinusoidal heart rate traces were detected in 8 patients, 6 of whom died; the 2 survivors showed evidence of gross cerebral damage. It is felt that the origin of the sinusoidal curve is probably central and reflects loss of central control of heart rate.

Female↗
PubMed1977

X-ray analysis and circular dichroism of the acid protease from Endothia parasitica and chymosin.

The structure of an acid proteinase from Endothia parasitica has been solved by x-ray diffraction using multiple isomorphous replacement. A 3 A resolution map was interpreted in terms of a bilobal structure with a long 25 A cleft. The secondary structure is mostly distorted beta-sheet. The circular dichroism was measured and model curves for different secondary structures were fitted by least squares indicating a large component of beta-structure. The structure was seen to be homologous with that of the acid proteinase from R. Chinensis and hence with pepsin and chymosin. A rotation function against diffraction data from chymosin crystals confirm confirm this and suggested an approach to the solution of this structure.

Ascomycota↗
PubMed1976

Purification and characterization of two lectins from Caragana arborescens seeds.

A glycoprotein fraction with hemagglutinating activity was purified by affinity chromatography from seeds of the pea tree, Caragana arborescens. Subsequent fractionation resolved two components, which could be separated on a preparative scale using different affinity matrices. The major component binds to N-acetylgalactosamine coupled to Sepharose 4B. It is a glycoprotein with high hemagglutinating activity. It is composed of two types of polypeptides, present in nonstoichiometric amounts, with apparent molecular weights near 30,000. In the native molecule, the subunits are cross-linked by disulfide bonds to form dimers, which in turn appear to be in rapid equilibrium with tetramers. The minor component binds to underivatized Sepharose 4B. It too, is a glycoprotein but has low hemagglutinating activity. It is composed of three types of polypeptides which, although they have apparent molecular weights near 30,000 are distinguished from the subunits of the major hemagglutinin by a number of physical and chemical properties. The native molecule is dimeric, with a mass of 60,000 daltons. The major component has high affinity (K = 0.1 mM) for the haptenic sugar, N-acetylgalactosamine, but will also bind D-galactose. Neither lectin has ABO blood group specificity, nor are they transformed mouse fibroblasts to the same extent.

Acetylgalactosamine↗
PubMed1969

Encephalitogenic protein: structure.

Amino acid sequences of encephalitogenic proteins from bovine cord and rabbit brain are reported. The bovine protein contains 45 residues. The rabbit protein is identical except for two isopolar substitutions, a dipeptide and amino acid deletion. Analysis of this protein and a 140-residue myelin basic protein indicates that the smaller protein is a portion of the larger encephalitogen. The larger myelin protein contains at least two encephalitogenic sites.

Amino Acid Sequence↗