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Biomedical subjects

D A Kaiser

Publications and source records attributed to D A Kaiser.

At least 37 records · Page 2Linked to original sources
PubMed1998

The effect of sprue design on the marginal accuracy of titanium castings.

The purpose of this study was to measure the effects of sprue number and position on cast titanium crown margins. Twenty-four complete veneer crown wax patterns were fabricated on a stainless steel die with a 30 degrees bevel finish line. Twelve wax patterns were sprued with one 8-gauge wax sprue and the remaining 12-gauge double sprued. All patterns were invested with a phosphate bonded investment. Castings were made with a titanium casting machine following the manufacturer's instructions and using commercially pure titanium (> 99.5%) ingots. The castings were than carefully cleansed and the margins were examined with indirect impression technique. Data were analysed with an ANOVA and the Student's t-test with confidence level at 95%. The results revealed that the marginal discrepancy for the double sprueing group (32.1 +/- 12.8 microm) has significantly less discrepancy (P < 0.001) than the single sprueing group (49.8 +/- 16.4 microm). There was no statistically significant differences in marginal discrepancy between locations within the sprueing techniques (P > 0.05). An improvement in the degree of casting accuracy of titanium crown was indicated by the double sprue design used in this investigation.

Analysis of Variance↗
PubMed1998

Designs for cast metal restorations.

This article reviewed clinical conditions that assist selection of specific design decisions for the tooth preparation for cast metal restorations. This decision should result in a conservative restoration for a given clinical situation. A paradigm is included to assist the dentist in the decision-making process.

Crowns↗
PubMed1998

The evolution of temporary fixed splints--the A-splint.

This article presents a review of the evaluation of the temporary splint leading up to the present-day acid-etched composite, wire-reinforced, internal splint called the "A-splint." Nine general uses for the A-splint in the modern dental practice and some common problems are presented.

Dental Care↗
PubMed1997

A substitute for facial replica in mannequin procedures.

The use of mannequin exercises has been a teaching tool in the education of dental students. Various commercially available materials to simulate extraoral facial structure form part of this apparatus, also called a "phantom head." It is not always practical, with cost considerations, to replace this external component when unavoidable wear and tear occurs. An alternative that uses a recycled milk carton is presented as an inexpensive substitute.

Dental Prosthesis Design↗
PubMed1996

Structural requirements and thermodynamics of the interaction of proline peptides with profilin.

The binding to poly(L-proline) is used for the affinity purification of profilins, but little is known about the structural and thermodynamic aspects of the interaction. We used changes in the intrinsic fluorescence of profilin, CD spectroscopy, and isothermal titration calorimetry to assess how the size and composition of synthetic proline-rich peptides influence binding to Acanthamoeba and human profilins. Although a 6 residue type II poly(L-proline) helix can span the binding site, highest affinity binding is achieved by proline oligomers > or = 10 residues. Binding is stereospecific since (D-proline)11 does not bind. In 75 mM KCI the dissociation equilibrium constant for poly(L-proline) is about 10 microM proline decamer units for amoeba profilin and 20-30 microM for human profilin. Consistent with a significant hydrophobic component of the interaction, delta Cp is negative and higher salt concentrations enhance the affinity. No protons dissociate or bind during the interaction. Binding of poly(L-proline) is favored both entropically and enthalpically. Substitution of glycine in proline undecamers reduces affinity by about 1 kcal mol-1 for each substitution due to increased rotational freedom of the free peptides. Substitution of alanine has a similar effect. Disorder in the free peptides imparts an unfavorable entropic cost for immobilizing the substituted peptides on the binding site on profilin.

Acanthamoeba↗
PubMed1996

Characterization of actin and poly-L-proline binding sites of Acanthamoeba profilin with monoclonal antibodies and by mutagenesis.

We characterized several deletion and substitution mutations of Acanthamoeba profilin and nine monoclonal antibodies to Acanthamoeba profilin. The results provide two independent lines of evidence about the binding sites for actin and poly-L-proline on the profilin molecule. This new evidence is consistent with the main conclusions about these binding sites from previous structural and mutagenic studies. Mutagenesis also revealed that the native structure of profilin is very sensitive to substitutions and deletions at the C terminus. For example, profilin with a deletion of the eight C-terminal residues has many of the physical properties of a molten globule, yet remarkably still binds to actin. This instability may account for the lack of function of similar mutants in yeast.

Acanthamoeba↗
PubMed1995

Recurrence of mandibular tori after surgical removal: two case reports.

Mandibular tori are sometimes removed to enhance periodontal and prosthodontic treatment. The exact cause of these benign bony overgrowths is not well understood, and therefore, their potential to recur after removal is also uncertain. Two case reports are presented in this article that provide evidence that at least some mandibular tori recur after surgical removal. One patient was followed-up for 11 years, and the other patient was followed-up for 14 years.

Exostoses↗
PubMed1994

Assessment of gingival margin thickness before margin placement.

Matrix material can be cut and placed beneath the gingival tissue to mimic a metal collar on a metal/ceramic crown restoration. If this metal matrix causes a discoloration of the gingival tissue, it would be wise to restore the tooth by using an all-porcelain margin.

Crowns↗
PubMed1994

Stereoselectivity in the epoxidation and cis-hydroxylation of 16-methylene-estra-1,3,5(10)-trienes.

Epoxidation of 3-methoxy-16-methylene-estra-1,3,5(10)-trien-17-one in the presence of alkaline hydrogen peroxide gives rise to (16R)- and (16S)-spiro[3- methoxy-17-oxoestra-1,3,5(10)-triene-16,2'-oxirane] in similar proportions. Epoxidation of the corresponding 16-methylene 17 beta-alcohol and 16-methylene-17 beta-acetate with m-chloroperbenzoic acid does not display any significant directing effects associated with allylic functionality, whereas Sharpless epoxidation of the 16-methylene 17 beta-alcohol is highly stereoselective, leading exclusively to the (16R) isomer. cis-Hydroxylation of the 16-methylene 17-ketone with osmium tetroxide/4-methylmorpholine-4-oxide proceeds stereoselectively to give mainly 16 alpha-hydroxy-16 beta-hydroxymethyl-3-methoxyestra-1,3,5(10)-trien-17-one. The isomeric addition products derived from these reactions are correlated by appropriate interconversions, and the assignments are corroborated by comparative reactivity of derived products.

Epoxy Compounds↗
PubMed1994

Multiband topographic EEG analysis of a simulated visuomotor aviation task.

Topographic EEG spectral magnitudes from 19 cortical sites were compared in 15 adult male subjects during performance of a simulated flight task and during control conditions which attempted to separately evaluate functional components of this task. Four conditions were studied, including eyes closed, a visual control, a motor control and a simulated landing task requiring integration of both visual and motor components. Each condition was repeated twice in a counterbalanced replicated measures design. A linked-ear EEG reference was used and spectral magnitudes calculated for 6 frequency bands. Decisions concerning band width and spectral transform were empirically determined. Findings indicated no significant differences between replications. A broad posterior cortical suppression of all frequencies was observed in the visual control condition. Anterior sites were affected only in the 7-12 Hz range. Additional suppression was seen during the motor control condition but limited to frontocentral sites in the 11-13 Hz band. The flight task, however, produced a further suppression at centroparietal cortex in the 9-13 Hz range. The extraction of both attentional and motor components from this task suggests that the parietal EEG activation was specific to cognitive processing.

Adult↗
PubMed1994

Evolution of removable partial denture design.

This is a brief overview of the progress of design philosophies of removable partial dentures. It begins in 1711 with the first published description of a removable partial denture prosthesis and continues, with discussion of the most significant discoveries, through 1990.

Dental Clasps↗
PubMed1993

Primary structure of and studies on Acanthamoeba actophorin.

We determined the amino acid sequence of the actin monomer binding/actin filament severing protein actophorin from Acanthamoeba castellanii by automated Edman degradation of peptide fragments and by sequencing of full-length cDNA. Actophorin consists of 138 amino acids (calculated molecular weight of 15,543) and shares a high degree of sequence similarity to other low molecular weight actin monomer sequestering proteins, especially vertebrate cofilin, vertebrate actin depolymerizing factor/destrin, and echinoderm depactin. Actophorin is smaller and does not contain a nuclear localization sequence like the related vertebrate proteins. Southern blot analysis indicates that actophorin is a single-copy gene; however, Northern blots show two distinct mRNA species of 1 and 0.9 kb in size. Homogeneous recombinant actophorin purified from Escherichia coli is indistinguishable from the native protein in its physical properties and in biochemical assays of its interaction with actin, but is less reactive with three monoclonal antibodies raised against the native protein. The NH2 terminus of native actophrin is blocked, while the initiating methionine residue is removed from recombinant actophorin. This difference has no measurable effect on activity. By fluorescent antibody staining of Acanthamoeba, actophorin colocalizes with actin filaments in the cortical cytoplasm, especially at the leading edge of the cell. Additionally, actophorin binds phosphatidylinositol 4',5'-bisphosphate. The recombinant actophorin forms X-ray diffraction quality crystals of superior quality in poly(ethylene glycol)/2-propanol and, like the native crystal form, belongs to space group P2(1)2(1)2(1).

Acanthamoeba↗
PubMed1993

Evolution of occlusion and occlusal instruments.

All occlusal concepts are based, in part, on theory, and all theories may have borrowed from the past. This article reviews the evolution of occlusal concepts to understand how differing theories interrelate, where they agree, and where each concept contributed to the ongoing understanding and evolution of occlusion principles. Also, the flexible and practical concept of biologic occlusion is presented. The philosophy of biologic occlusion is one that functions in health. The goals of biologic occlusion are also presented.

Centric Relation↗
PubMed1991

Shear bond strength of two resin adhesives for acid-etched metal prostheses.

This study compared the shear bond strength of Panavia EX and Comspan Opaque adhesive resins with electrolytically etched or sandblasted Rexillium III or Litecast B metals bonded to extracted teeth. An analysis of variance revealed that there is no difference in bonding strength among etched or sandblasted Rexillium III metal with either Panavia EX or Comspan Opaque resins. With Litecast B metal, sandblasting produced a greater bond strength than etching with Panavia Ex resin (38.19 MPa sandblasted; 30.53 MPa etched). Conversely, Comspan Opaque resin had a value of 30.10 MPa etched and 15.40 MPa sandblasted. The etched Rexillium III and Panavia EX resins recorded a greater bond strength (38.38 MPa) than Comspan Opaque resin (27.83 MPa) or sandblasted Rexillium III metal (Rexillium III 34.74 MPa; Comspan Opaque 20.39 MPa) and Litecast B metal (Panavia EX 38.19 MPa; Comspan Opaque 15.40 MPa). Eighty percent of the failures occurred at the cement-metal interface with both cements.

Acid Etching, Dental↗
PubMed1991

Comparison of resistance features for complex amalgam restorations.

This study evaluated the resistance provided to complex Dispersalloy amalgam restorations by pins (Group 1), amalgapins (Group 2), and a peripheral shelf or shoulder (Group 3) or in combinations of pins plus peripheral shelf (Group 4), or amalgapins plus peripheral shelf (Group 5). The occlusal surfaces of 50 extracted maxillary molar teeth were ground to a flat surface 2 mm occlusal to the CEJ, and the roots were matched and embedded in acrylic resin 2 mm apical to the CEJ. The greatest faciolingual and mesiodistal dimensions of each tooth at the level of preparation were recorded and these two measurements were multiplied to give a product for each specimen. The teeth were then sorted by tooth sizes and equally distributed among the five groups. Each group of flattened teeth received a different resistance form configuration. Amalgam was condensed using a matrix; the bands and excess amalgam were removed 24 hours later and each amalgam "occlusal" surface was ground flat to standardize the restoration at a 4 mm occlusal height. A 1 mm 45 degrees bevel was prepared on the facio-occlusal angle of the amalgam, and each specimen was loaded in compression at 45 degrees in an Instron at a crosshead speed of 1 mm/min. The groups and their mean (SD) failure loads in Newtons were: Group 1: 1515 (274); Group 2: 1521 (244); Group 3: 578 (175); Group 4: 1199 (229); and Group 5: 1691 (298). A one-factor ANOVA and a Tukey B post-hoc analysis showed no differences between Groups 1, 2 and 5.(ABSTRACT TRUNCATED AT 250 WORDS)

Analysis of Variance↗
PubMed1990

Identification of functional regions on the tail of Acanthamoeba myosin-II using recombinant fusion proteins. I. High resolution epitope mapping and characterization of monoclonal antibody binding sites.

We used a series of COOH-terminally deleted recombinant myosin molecules to map precisely the binding sites of 22 monoclonal antibodies along the tail of Acanthamoeba myosin-II. These antibodies bind to 14 distinguishable epitopes, some separated by less than 10 amino acids. The positions of the binding sites visualized by electron microscopy agree only approximately with the physical positions of these sites on the alpha-helical coiled-coil tail. On the other hand, the epitope map agrees precisely with competitive binding studies: all antibodies that share an epitope compete with each other for binding to myosin. Antibodies with adjacent epitopes can compete with each other at linear distances up to 5 or 6 nm, and many antibodies that bind 3-7-nm apart can enhance the binding of each other to myosin. Most of the antibodies that bind to the distal 37 nm of the tail disrupt assembly of octameric minifilaments and, depending upon the exact location of the binding site, stop assembly at specific steps yielding, for example, monomers, antiparallel dimers, parallel dimers or antiparallel tetramers. The effects of these antibodies on assembly identify sites on the tail that are required for individual steps in minifilament assembly. Experiments on the assembly of truncated myosin-II tails have revealed a complementary group of sites that participate in the assembly reactions (Sinard, J.H., D.L. Rimm, and T.D. Pollard. 1990. J. Cell Biol. 111:2417-2426). Antibodies that bind to the distal tail but do not affect assembly appear to have a low affinity for myosin-II. Antibodies that bind to the proximal 50 nm of the tail do not inhibit the assembly of minifilaments. Many antibodies that bind to the tail of myosin-II, even some that have no obvious effect on minifilament assembly, can inhibit the actomyosin ATPase activity and the contraction of an actin gel formed in crude extracts. An antibody that binds between amino acids 1447 and 1467 inhibits the phosphorylation of serine residues distal to residue 1483.

Acanthamoeba↗
PubMed1989

Characterization of renatured profilin purified by urea elution from poly-L-proline agarose columns.

We present evidence that native profilin can be purified from cellular extracts of Acanthamoeba, Dictyostelium, and human platelets by affinity chromatography on poly-L-proline agarose. After applying cell extracts and washing the column with 3 M urea, homogeneous profilin is eluted by increasing the urea concentration to 6-8 M. Acanthamoeba profilin-I and profilin-II can subsequently be separated by cation exchange chromatography. The yield of Acanthamoeba profilin is twice that obtained by conventional methods. Several lines of evidence show that the profilins fully renature after removal of the urea by dialysis: 1) dialyzed Acanthamoeba and human profilins rebind quantitatively to poly-L-proline and bind to actin in the same way as native, conventionally purified profilin without urea treatment; 2) dialyzed profilins form 3-D crystals under the same conditions as native profilins; 3) dialyzed Acanthamoeba profilin-I has an NMR spectrum identical with that of native profilin-I; and 4) dialyzed human and Acanthamoeba profilins inhibit actin polymerization. We report the discovery of profilin in Dictyostelium cell extracts using the same method. Based on these observations we conclude that urea elution from poly-L-proline agarose followed by renaturation will be generally useful for preparing profilins from a wide variety of cells. Perhaps also of general use is the finding that either myosin-II or alpha-actinin in crude cell extracts can be bound selectively to the poly-L-proline agarose column depending on the ionic conditions used to equilibrate the column. We have purified myosin-II from both Acanthamoeba and Dictyostelium cell extracts and alpha-actinin from Acanthamoeba cell extracts in the appropriate buffers. These proteins are retained as complexes with actin by the agarose and not by a specific interaction with poly-L-proline. They can be eluted by dissociating the complexes with ATP and separated from actin by gel filtration if necessary.

Acanthamoeba↗