PubMed Health⌕ Search

Biomedical subjects

J S Jacob

Publications and source records attributed to J S Jacob.

32 records · Page 2Linked to original sources
PubMed1985

Corneal thickness changes following cataract surgery: effect of lens implantation and sodium hyaluronate.

Consecutive patients undergoing intracapsular cataract surgery with and without lens implantation were included in one of three groups of fifteen patients for postoperative corneal thickness measurement. One group underwent cataract extraction alone, another group had cataract extraction and lens implantation using iris supported posterior chamber implants, and another group underwent lens implantation with the use of sodium hyaluronate to reform the anterior chamber after cataract extraction. Maximal increase in corneal thickness occurred within the first 24 hours of surgery in all groups. No significant difference in corneal thickness between the implant and non-implant group was found at any time. When sodium hyaluronate was used to reform the anterior chamber prior to lens implantation the increase in corneal thickness was significantly less than in the group not on sodium hyaluronate (0.01 less than p less than 0.02 on the third postoperative day). In the long term all patients' corneas returned to preoperative levels within 28 days of surgery.

Anthropometry↗
PubMed1985

Two-dimensional crystals of a membrane protein: arrangement of subunits within the crystal sheet.

Two-dimensional crystals have been prepared from the photosynthetic reaction center of Rhodopseudomonas viridis. Filtered images of these crystals show individual subunits approximately 4.5 nm in diameter arranged at a center-to-center distance of 6.4 nm. Our previous studies suggested that each subunit within such a sheet corresponds to a single photosynthetic reaction center. Air-dried and freeze-etched shadowed preparations of the crystals yield images which are quite different from negatively stained material. Rotary-shadowed surfaces of the crystals show rows of wedge-shaped particles separated by 3 nm furrows. Two such wedge-shaped particles occupy the 12.1 X 12.9 nm area in which four negatively stained subunits are normally visualized. Close analysis of these shadowed pictures suggests that both the shadowed and negatively stained images can be accounted for by a single model of subunit arrangement within the crystal. Within each 12.1 X 12.9 nm unit cell, two subunits are placed near one surface of the sheet, and two others are near the other surface. All four subunits are visible in negative stain. When the surface is shadowed, only the two subunits which project above the surface of the sheet accumulate appreciable amounts of the heavy metal shadow. Because of their close position, one subunit shades the other, forming the wedge-shaped appearance characteristic of the crystal. The only arrangement consistent with both shadowed and negatively stained images is one in which the two raised subunits occupy positions at either end of a diagonal across the unit cell. The analysis of shadowed images indicates that the plane group of the crystals is P22(1)2(1).

Bacterial Proteins↗
PubMed1984

Structure of a bacterial photosynthetic membrane: integrity of reaction centers following proteolysis and detergent solubilization.

The photosynthetic membranes of the purple bacterium Rhodopseudomonas viridis are composed of a semi-crystalline lattice of subunits. Proteolysis of isolated membranes with trypsin or pronase results in the degradation of polypeptides associated with the photosynthetic reaction center. However, two low molecular weight peptides which may form the light-harvesting complex survive the enzymatic treatment. The proteolysis does not affect the major absorbance peak (830 nm) associated with the reaction center. However, treatment of proteolyzed membranes with detergents such as LDAO abolishes the 830 nm absorbance peak. The 830 nm peak is stable following LDAO solubilization of non-proteolyzed membranes. These results suggest that a combination of covalent and non-covalent interactions are important in maintaining the configuration of the reaction center, and are consistent with a model of membrane organization in which the light-harvesting components are buried in a lipid phase of the membrane and reaction center components form the large structures which electron microscope studies have shown to extend from either membrane surface.

Bacterial Proteins↗
PubMed1984

Photosynthetic reaction centers in artificial membranes: estimating protein dimensions by freeze-fracture and freeze-etching.

Because estimates of size and shape for membrane proteins are difficult to obtain directly, many workers have incorporated purified proteins into artificial lipid bilayers. Freeze-fracturing has then been used to provide a measure of the approximate size and shape of the membrane protein. We have formed reconstituted membranes containing the photosynthetic reaction center of Rhodopseudomonas viridis, a photosynthetic bacterium. The size and shape of this reaction center is accurately known from studies of negatively stained crystals of the protein to be approximately 4.5 X 6.0 nm. Freeze-fracture images of the reaction center in phosphatidyl choline liposomes show particles formed after reconstitution with an average diameter of 12.3 nm, much larger than the actual size of the protein. Deep-etched images of the surfaces of the liposomes, in which each individual reaction center complex can be seen clearly, show why the diameter of the protein is exaggerated in freeze-fracture. The individual reaction centers tend to cluster into large groups, allowing several individual reaction centers to be visualized as a single (much larger) particle in freeze-fracture. Freeze-fracturing, although a valuable tool in the analysis of membrane structure in natural and artificial membranes, must be used with caution in the estimation of molecular sizes and shapes.

Bacterial Proteins↗
PubMed1983

Structure of a bacterial photosynthetic membrane. Isolation, polypeptide composition, and selective proteolysis.

A procedure for the isolation of highly purified bacterial photosynthetic membranes from Rhodopseudomonas viridis is described. The purity of the final membrane fraction has been confirmed by electron microscopy. Seven major polypeptide bands are associated with the photosynthetic membranes, and all seven are resistant to solubilization in Triton X-100 detergent. Two pigmented bands with apparent molecular weights of 44K and 41K are thought to be cytochromes. The three polypeptides with apparent molecular weights of 38K, 32K, and 28K have been reported in reaction center preparations of other laboratories. Two low-molecular-weight (16K and 11K) bands bind bacteriochlorophyll b and may represent light-harvesting bacteriochlorophyll-protein complexes. The structures that were isolated seem to represent complete photosynthetic membranes, consisting of reaction center, electron transport, and light-harvesting components, all arranged in the regular lattice characteristic of viridis. Selective proteolysis of these membranes indicates that all membrane components are accessible to digestion by trypsin and pronase, except for the light-harvesting complexes.

Bacterial Proteins↗
PubMed1983

Two-dimensional crystals formed from photosynthetic reaction centers.

Photosynthetic reaction centers from the bacterium Rhodopseudomonas viridis were prepared after detergent solubilization of photosynthetic membranes. The purified reaction centers, in agreement with reports from other laboratories, contain four distinct polypeptides ranging in molecular weight from 28,000 to 41,000. When the detergent was gradually removed by dialysis under appropriate conditions, large two-dimensional sheets of reaction centers were formed, suitable for analysis by electron microscopy. The crystals were rectangular, and the dimensions of a single unit cell were 121 X 129 A. Each unit cell contained four distinct subunits, each with approximate dimensions of 45 X 60 A. The thickness of the sheet was 60 A. Preliminary studies of the sheets with negative staining indicated that the sheets show a high degree of order: as many as six orders are visible in transforms of the images. Because of the fact that in R. viridis the native membrane from which these reaction centers were purified also displays a crystal-like structure, comparative studies between a membrane and one of its components, each analyzed by Fourier techniques, are now possible.

Bacterial Proteins↗
PubMed1982

Report on the presence of a toxic substance, dimethyl formamide, in sodium fluorescein used for fluorescein angiography.

The revelation that intravenous sodium fluorescein is not all that it might seem to be may be a significant finding in the light of the adverse reactions to fluorescein that have been previously reported. Analysis of commercially prepared intravenous sodium fluorescein by mass spectroscopy and nuclear magnetic resonance has indicated that an industrial solvent used in the manufacturing process has not been eliminated. Dimethyl formamide is an industrial solvent with a maximum acceptable exposure level of 10 parts per million for dermal contact. It has been found in quantities of 5000 parts per million in the fluorescein for intravenous use. This investigation was prompted by a significant increase in the adverse reactions in patients receiving intravenous fluorescein in the retinal photographic unit at the Manchester Royal Eye Hospital.

Dimethylformamide↗
PubMed1981

Some factors affecting the lipid secretory phase of fat absorption by intestine in vitro from golden hamster.

We studied the secretory phase of fat absorption by sacs of the everted intestine in vitro when long chain fatty acid and monoglyceride had been taken up from a physicochemically defined bile salt micellar solution. After uptake, a sac received a supplemental incubation in a saline solution without added lipid. The presence of calcium ion in the medium during supplemental incubation was essential for the production and release of resynthesized triglyceride in the form of chylomicrons. The particles appeared to enter the serosal fluid via the lacteals. The rate of secretion of the lipid varied directly with the concentration of calcium ion in the mucosal fluid in the range 100-900 microM. At a given concentration in the serosal or mucosal fluid, the calcium ion in the latter fluid had the greater effect. The study of additional factors included the original location of the segment in the intestine of the living animal, temperature, use of D2O instead of water, and the effects of Ba2+, Sr2+, Mg2+, and La3+ on lipid secretion.

Animals↗
PubMedDate not supplied

Cytokines delivered by biodegradable microspheres promote effective suppression of human tumors by human peripheral blood lymphocytes in the SCID-Winn model.

A new technology for the local and sustained delivery of immunostimulatory molecules to the tumor environment for cancer immunotherapy was evaluated. The ability of cytokines delivered by biodegradable microspheres to promote the antitumor activity of human peripheral blood lymphocytes (PBL) was tested in a human PBL, human tumor, and SCID mouse (SCID-Winn) model. Co-engraftment of human recombinant IL-12-loaded microspheres with human PBL and tumors in SCID mice promoted complete tumor suppression in as many as 100% of the mice, whereas microspheres loaded with polyethyleneglycol-interleukin-2 suppressed but did not eliminate the growth of tumor xenografts. Control microspheres (loaded with bovine serum albumin) in the presence of human PBL or cytokine-loaded microspheres in the absence of human PBL had no tumor-suppressive effect. Coincident with the enhancement of the human PBL-mediated antitumor activity in mice treated with IL-12-loaded microspheres was the production and release of human IFN-gamma indicating that IL-12 released from the microspheres results in the activation of the engrafted human PBL. The results establish that biodegradable microspheres represent an effective tool for the local and sustained delivery of cytokines to the tumor environment for cancer immunotherapy.

Adjuvants, Immunologic↗
PubMedDate not supplied

A relative cost-effectiveness analysis of different methods of screening for diabetic retinopathy.

The relative cost and cost-effectiveness of different methods of screening diabetic patients for sight-threatening retinopathy are assessed. The resource costs per screening visit, both to the health service and to patients, of ophthalmoscopic examination by primary screeners including general practitioners, hospital physicians, and ophthalmic opticians are estimated together with those of a similar screening test by ophthalmological clinical assistants. The total resource cost per screen of screening using non-mydriatic photography is also estimated. Using estimates of sensitivity, specificity, and prevalence generated in the screening of 3318 diabetic patients in three UK centres, the relative cost-effectiveness of screening methods is estimated in terms of their cost per true positive case detected. On the assumption that a patient makes a special trip for eye screening, the cost per true positive case detected for primary screeners ranges from 633 pounds for a GP-screened group in one centre to 1079 pounds for another GP-screened group in a second centre; the cost per true positive case detected of photography ranges from 497 pounds for a camera that is taken to general practices in one centre to 1546 pounds for a hospital-based camera. Relative cost-effectiveness changes if, in some contexts, the screening can take place without requiring an additional patient visit, and is strongly related to the relative sensitivity of the screening methods and to the prior probability (prevalence or incidence) of retinopathy in the diabetic population.

Cost-Benefit Analysis↗